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Wikipedia

CD79A

January 01, 1970

Cluster of differentiation CD79A also known as B-cell antigen receptor complex-associated protein alpha chain and MB-1 membrane glycoprotein, is a protein that in humans is encoded by the CD79A gene.[5]

CD79A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCD79A, IGA, MB-1, CD79a molecule, MB1, IGAlpha
External IDsOMIM: 112205; MGI: 101774; HomoloGene: 31053; GeneCards: CD79A; OMA:CD79A - orthologs
Orthologs
SpeciesHumanMouse
Entrez

973

12518

Ensembl

ENSG00000105369

ENSMUSG00000003379

UniProt

P11912

P11911

RefSeq (mRNA)

NM_021601
NM_001783

NM_007655

RefSeq (protein)

NP_001774
NP_067612

NP_031681

Location (UCSC)Chr 19: 41.88 – 41.88 MbChr 7: 24.6 – 24.6 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

The CD79a protein together with the related CD79b protein, forms a dimer associated with membrane-bound immunoglobulin in B-cells, thus forming the B-cell antigen receptor (BCR). This occurs in a similar manner to the association of CD3 with the T-cell receptor, and enables the cell to respond to the presence of antigens on its surface.[6]

It is associated with agammaglobulinemia-3.[7]

Gene edit

The mouse CD79A gene, then called mb-1, was cloned in the late 1980s,[8] followed by the discovery of human CD79A in the early 1990s.[9][10] It is a short gene, 4.3 kb in length, with 5 exons encoding for 2 splice variants resulting in 2 isoforms.[5]

CD79A is conserved and abundant among ray-finned fish (actinopterygii) but not in the evolutionarily more ancient chondrichthyes such as shark.[11] The occurrence of CD79A thus coincides with the evolution of B cell receptors with greater diversity generated by recombination of multiple V, D, and J elements in bony fish contrasting the single V, D and J elements found in shark.[12]

Structure edit

CD79a is a membrane protein with an extracellular immunoglobulin domain, a single span transmembrane region and a short cytoplasmic domain.[5] The cytoplasmic domain contains multiple phosphorylation sites including a conserved dual phosphotyrosine binding motif, termed immunotyrosine-based activation motif (ITAM).[13][14] The larger CD79a isoform contains an insert in position 88-127 of human CD79a resulting in a complete immunoglobulin domain, whereas the smaller isoform has only a truncated Ig-like domain.[5] CD79a has several cysteine residues, one of which forms covalent bonds with CD79b.[15]

Function edit

CD79a plays multiple and diverse roles in B cell development and function. The CD79a/b heterodimer associates non-covalently with the immunoglobulin heavy chain through its transmembrane region, thus forming the BCR along with the immunoglobulin light chain and the pre-BCR when associated with the surrogate light chain in developing B cells. Association of the CD79a/b heterodimer with the immunoglobulin heavy chain is required for surface expression of the BCR and BCR induced calcium flux and protein tyrosine phosphorylation.[16] Genetic deletion of the transmembrane exon of CD79A results in loss of CD79a protein and a complete block of B cell development at the pro to pre B cell transition.[17] Similarly, humans with homozygous splice variants in CD79A predicted to result in loss of the transmembrane region and a truncated or absent protein display agammaglobulinemia and no peripheral B cells.[7][18][19]

The CD79a ITAM tyrosines (human CD79a Tyr188 and Tyr199, mouse CD79a Tyr182 and Tyr193) phosphorylated in response to BCR crosslinking, are critical for binding of Src-homology 2 domain-containing kinases such as spleen tyrosine kinase (Syk) and signal transduction by CD79a.[20][21] In vivo, the CD79a ITAM tyrosines synergize with the CD79b ITAM tyrosines to mediate the transition from the pro to the pre B cell stage as suggested by the analysis of mice with targeted mutations of the CD79a and CD79b ITAM.[22][23] Loss of only one of the two functional CD79a/b ITAMs resulted in impaired B cell development but B cell functions such as the T cell independent type II response and BCR mediated calcium flux in the available B cells were intact. However, the presence of both the CD79a and CD79b ITAM tyrosines were required for normal T cell dependent antibody responses.[22][24] The CD79a cytoplasmic domain further contains a non-ITAM tyrosine distal of the CD79a ITAM (human CD79a Tyr210, mouse CD79a Tyr204) that can bind BLNK and Nck once phosphorylated,[25][26][27] and is critical for BCR mediated B cell proliferation and B1 cell development.[28] CD79a ITAM tyrosine phosphorylation and signaling is negatively regulated by serine and threonine residues in direct proximity of the ITAM (human CD79a Ser197, Ser203, Thr209; mouse CD79a Ser191, Ser197, Thr203),[29][30] and play a role in limiting formation of bone marrow plasma cells secreting IgG2a and IgG2b.[23]

Diagnostic relevance edit

The CD79a protein is present on the surface of B-cells throughout their life cycle, and is absent on all other healthy cells, making it a highly reliable marker for B-cells in immunohistochemistry. The protein remains present when B-cells transform into active plasma cells, and is also present in virtually all B-cell neoplasms, including B-cell lymphomas, plasmacytomas, and myelomas. It is also present in abnormal lymphocytes associated with some cases of Hodgkins disease. Because even on B-cell precursors, it can be used to stain a wider range of cells than can the alternative B-cell marker CD20, but the latter is more commonly retained on mature B-cell lymphomas, so that the two are often used together in immunohistochemistry panels.[6]

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105369 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003379 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d "Entrez Gene: CD79A CD79a molecule, immunoglobulin-associated alpha".
  6. ^ a b Anthony S-Y L, Cooper K, Leong FJ (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. pp. XX. ISBN 1-84110-100-1.
  7. ^ a b Online Mendelian Inheritance in Man (OMIM): 613501
  8. ^ Sakaguchi N, Kashiwamura S, Kimoto M, Thalmann P, Melchers F (Nov 1988). "B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like structural properties". The EMBO Journal. 7 (11): 3457–64. doi:10.1002/j.1460-2075.1988.tb03220.x. PMC 454845. PMID 2463161.
  9. ^ Ha HJ, Kubagawa H, Burrows PD (Mar 1992). "Molecular cloning and expression pattern of a human gene homologous to the murine mb-1 gene". Journal of Immunology. 148 (5): 1526–31. doi:10.4049/jimmunol.148.5.1526. PMID 1538135. S2CID 22129592.
  10. ^ Flaswinkel H, Reth M (1992). "Molecular cloning of the Ig-alpha subunit of the human B-cell antigen receptor complex". Immunogenetics. 36 (4): 266–9. doi:10.1007/bf00215058. PMID 1639443. S2CID 28622219.
  11. ^ Sims R, Vandergon VO, Malone CS (Mar 2012). "The mouse B cell-specific mb-1 gene encodes an immunoreceptor tyrosine-based activation motif (ITAM) protein that may be evolutionarily conserved in diverse species by purifying selection". Molecular Biology Reports. 39 (3): 3185–96. doi:10.1007/s11033-011-1085-7. PMC 4667979. PMID 21688146.
  12. ^ Flajnik MF, Kasahara M (Jan 2010). "Origin and evolution of the adaptive immune system: genetic events and selective pressures". Nature Reviews Genetics. 11 (1): 47–59. doi:10.1038/nrg2703. PMC 3805090. PMID 19997068.
  13. ^ Reth M (Mar 1989). "Antigen receptor tail clue". Nature. 338 (6214): 383–4. Bibcode:1989Natur.338..383R. doi:10.1038/338383b0. PMID 2927501. S2CID 5213145.
  14. ^ Cambier JC (Oct 1995). "Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)". Journal of Immunology. 155 (7): 3281–5. doi:10.4049/jimmunol.155.7.3281. PMID 7561018. S2CID 996547.
  15. ^ Reth M (1992). "Antigen receptors on B lymphocytes". Annual Review of Immunology. 10 (1): 97–121. doi:10.1146/annurev.iy.10.040192.000525. PMID 1591006.
  16. ^ Yang, Jianying; Reth, Michael (September 2010). "Oligomeric organization of the B-cell antigen receptor on resting cells". Nature. 467 (7314): 465–469. Bibcode:2010Natur.467..465Y. doi:10.1038/nature09357. ISSN 1476-4687. PMID 20818374. S2CID 3261220.
  17. ^ Pelanda R, Braun U, Hobeika E, Nussenzweig MC, Reth M (Jul 2002). "B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig-alpha and Ig-beta". Journal of Immunology. 169 (2): 865–72. doi:10.4049/jimmunol.169.2.865. PMID 12097390.
  18. ^ Minegishi Y, Coustan-Smith E, Rapalus L, Ersoy F, Campana D, Conley ME (Oct 1999). "Mutations in Igalpha (CD79a) result in a complete block in B-cell development". The Journal of Clinical Investigation. 104 (8): 1115–21. doi:10.1172/JCI7696. PMC 408581. PMID 10525050.
  19. ^ Wang Y, Kanegane H, Sanal O, Tezcan I, Ersoy F, Futatani T, Miyawaki T (Apr 2002). "Novel Igalpha (CD79a) gene mutation in a Turkish patient with B cell-deficient agammaglobulinemia". American Journal of Medical Genetics. 108 (4): 333–6. doi:10.1002/ajmg.10296. PMID 11920841.
  20. ^ Flaswinkel H, Reth M (Jan 1994). "Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor". The EMBO Journal. 13 (1): 83–9. doi:10.1002/j.1460-2075.1994.tb06237.x. PMC 394781. PMID 8306975.
  21. ^ Reth M, Wienands J (1997). "Initiation and processing of signals from the B cell antigen receptor". Annual Review of Immunology. 15 (1): 453–79. doi:10.1146/annurev.immunol.15.1.453. PMID 9143696.
  22. ^ a b Gazumyan A, Reichlin A, Nussenzweig MC (Jul 2006). "Ig beta tyrosine residues contribute to the control of B cell receptor signaling by regulating receptor internalization". The Journal of Experimental Medicine. 203 (7): 1785–94. doi:10.1084/jem.20060221. PMC 2118343. PMID 16818674.
  23. ^ a b Patterson HC, Kraus M, Wang D, Shahsafaei A, Henderson JM, Seagal J, Otipoby KL, Thai TH, Rajewsky K (Sep 2011). "Cytoplasmic Ig alpha serine/threonines fine-tune Ig alpha tyrosine phosphorylation and limit bone marrow plasma cell formation". Journal of Immunology. 187 (6): 2853–8. doi:10.4049/jimmunol.1101143. PMC 3169759. PMID 21841126.
  24. ^ Kraus M, Pao LI, Reichlin A, Hu Y, Canono B, Cambier JC, Nussenzweig MC, Rajewsky K (Aug 2001). "Interference with immunoglobulin (Ig)alpha immunoreceptor tyrosine-based activation motif (ITAM) phosphorylation modulates or blocks B cell development, depending on the availability of an Igbeta cytoplasmic tail". The Journal of Experimental Medicine. 194 (4): 455–69. doi:10.1084/jem.194.4.455. PMC 2193498. PMID 11514602.
  25. ^ Engels N, Wollscheid B, Wienands J (Jul 2001). "Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha". European Journal of Immunology. 31 (7): 2126–34. doi:10.1002/1521-4141(200107)31:7<2126::aid-immu2126>3.0.co;2-o. PMID 11449366. S2CID 31494726.
  26. ^ Kabak S, Skaggs BJ, Gold MR, Affolter M, West KL, Foster MS, Siemasko K, Chan AC, Aebersold R, Clark MR (Apr 2002). "The direct recruitment of BLNK to immunoglobulin alpha couples the B-cell antigen receptor to distal signaling pathways". Molecular and Cellular Biology. 22 (8): 2524–35. doi:10.1128/MCB.22.8.2524-2535.2002. PMC 133735. PMID 11909947.
  27. ^ Castello A, Gaya M, Tucholski J, Oellerich T, Lu KH, Tafuri A, Pawson T, Wienands J, Engelke M, Batista FD (Sep 2013). "Nck-mediated recruitment of BCAP to the BCR regulates the PI(3)K-Akt pathway in B cells". Nature Immunology. 14 (9): 966–75. doi:10.1038/ni.2685. PMID 23913047. S2CID 2532325.
  28. ^ Patterson HC, Kraus M, Kim YM, Ploegh H, Rajewsky K (Jul 2006). "The B cell receptor promotes B cell activation and proliferation through a non-ITAM tyrosine in the Igalpha cytoplasmic domain". Immunity. 25 (1): 55–65. doi:10.1016/j.immuni.2006.04.014. PMID 16860757.
  29. ^ Müller R, Wienands J, Reth M (Jul 2000). "The serine and threonine residues in the Ig-alpha cytoplasmic tail negatively regulate immunoreceptor tyrosine-based activation motif-mediated signal transduction". Proceedings of the National Academy of Sciences of the United States of America. 97 (15): 8451–4. Bibcode:2000PNAS...97.8451M. doi:10.1073/pnas.97.15.8451. PMC 26968. PMID 10900006.
  30. ^ Heizmann B, Reth M, Infantino S (Oct 2010). "Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor". Proceedings of the National Academy of Sciences of the United States of America. 107 (43): 18563–8. Bibcode:2010PNAS..10718563H. doi:10.1073/pnas.1009048107. PMC 2972992. PMID 20940318.

Further reading edit

  • Herren B, Burrows PD (2003). "B cell-restricted human mb-1 gene: expression, function, and lineage infidelity". Immunologic Research. 26 (1–3): 35–43. doi:10.1385/IR:26:1-3:035. PMID 12403343. S2CID 38456117.
  • Leduc I, Preud'homme JL, Cogné M (Oct 1992). "Structure and expression of the mb-1 transcript in human lymphoid cells". Clinical and Experimental Immunology. 90 (1): 141–6. doi:10.1111/j.1365-2249.1992.tb05846.x. PMC 1554548. PMID 1395095.
  • Müller B, Cooper L, Terhorst C (Jun 1992). "Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29". European Journal of Immunology. 22 (6): 1621–5. doi:10.1002/eji.1830220641. PMID 1534761. S2CID 23910309.
  • Hutchcroft JE, Harrison ML, Geahlen RL (Apr 1992). "Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor". The Journal of Biological Chemistry. 267 (12): 8613–9. doi:10.1016/S0021-9258(18)42487-8. PMID 1569106.
  • Yu LM, Chang TW (Jan 1992). "Human mb-1 gene: complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes". Journal of Immunology. 148 (2): 633–7. doi:10.4049/jimmunol.148.2.633. PMID 1729378. S2CID 24075079.
  • Venkitaraman AR, Williams GT, Dariavach P, Neuberger MS (Aug 1991). "The B-cell antigen receptor of the five immunoglobulin classes". Nature. 352 (6338): 777–81. Bibcode:1991Natur.352..777V. doi:10.1038/352777a0. PMID 1881434. S2CID 4246284.
  • Kurosaki T, Johnson SA, Pao L, Sada K, Yamamura H, Cambier JC (Dec 1995). "Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling". The Journal of Experimental Medicine. 182 (6): 1815–23. doi:10.1084/jem.182.6.1815. PMC 2192262. PMID 7500027.
  • Lankester AC, van Schijndel GM, Cordell JL, van Noesel CJ, van Lier RA (Apr 1994). "CD5 is associated with the human B cell antigen receptor complex". European Journal of Immunology. 24 (4): 812–6. doi:10.1002/eji.1830240406. PMID 7512031. S2CID 25093082.
  • Vasile S, Coligan JE, Yoshida M, Seon BK (Apr 1994). "Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex". Molecular Immunology. 31 (6): 419–27. doi:10.1016/0161-5890(94)90061-2. PMID 7514267.
  • Brown VK, Ogle EW, Burkhardt AL, Rowley RB, Bolen JB, Justement LB (Jun 1994). "Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45". The Journal of Biological Chemistry. 269 (25): 17238–44. doi:10.1016/S0021-9258(17)32545-0. PMID 7516335.
  • Pani G, Kozlowski M, Cambier JC, Mills GB, Siminovitch KA (Jun 1995). "Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling". The Journal of Experimental Medicine. 181 (6): 2077–84. doi:10.1084/jem.181.6.2077. PMC 2192043. PMID 7539038.

External links edit

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

January 01, 1970
cd79a, cluster, differentiation, also, known, cell, antigen, receptor, complex, associated, protein, alpha, chain, membrane, glycoprotein, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1cv9identifiersalias. Cluster of differentiation CD79A also known as B cell antigen receptor complex associated protein alpha chain and MB 1 membrane glycoprotein is a protein that in humans is encoded by the CD79A gene 5 CD79AAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1CV9IdentifiersAliasesCD79A IGA MB 1 CD79a molecule MB1 IGAlphaExternal IDsOMIM 112205 MGI 101774 HomoloGene 31053 GeneCards CD79A OMA CD79A orthologsGene location Human Chr Chromosome 19 human 1 Band19q13 2Start41 877 279 bp 1 End41 881 372 bp 1 Gene location Mouse Chr Chromosome 7 mouse 2 Band7 A3 7 13 49 cMStart24 596 806 bp 2 End24 601 622 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inspleenlymph nodeappendixbone marrow cellsbloodrectumparotid glandthymussuperficial temporal arterythymusTop expressed inspleenbone marrowthymuscolonjejunumileumlungduodenummorulapancreasMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein binding transmembrane signaling receptor activity protein homodimerization activityCellular componentintegral component of membrane multivesicular body membrane raft plasma membrane membrane external side of plasma membrane cytoplasm B cell receptor complex integral component of plasma membraneBiological processB cell activation B cell proliferation cell surface receptor signaling pathway adaptive immune response immune system process B cell differentiation B cell receptor signaling pathway protein homotetramerizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez97312518EnsemblENSG00000105369ENSMUSG00000003379UniProtP11912P11911RefSeq mRNA NM 021601NM 001783NM 007655RefSeq protein NP 001774NP 067612NP 031681Location UCSC Chr 19 41 88 41 88 MbChr 7 24 6 24 6 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse The CD79a protein together with the related CD79b protein forms a dimer associated with membrane bound immunoglobulin in B cells thus forming the B cell antigen receptor BCR This occurs in a similar manner to the association of CD3 with the T cell receptor and enables the cell to respond to the presence of antigens on its surface 6 It is associated with agammaglobulinemia 3 7 Contents 1 Gene 2 Structure 3 Function 4 Diagnostic relevance 5 See also 6 References 7 Further reading 8 External linksGene editThe mouse CD79A gene then called mb 1 was cloned in the late 1980s 8 followed by the discovery of human CD79A in the early 1990s 9 10 It is a short gene 4 3 kb in length with 5 exons encoding for 2 splice variants resulting in 2 isoforms 5 CD79A is conserved and abundant among ray finned fish actinopterygii but not in the evolutionarily more ancient chondrichthyes such as shark 11 The occurrence of CD79A thus coincides with the evolution of B cell receptors with greater diversity generated by recombination of multiple V D and J elements in bony fish contrasting the single V D and J elements found in shark 12 Structure editCD79a is a membrane protein with an extracellular immunoglobulin domain a single span transmembrane region and a short cytoplasmic domain 5 The cytoplasmic domain contains multiple phosphorylation sites including a conserved dual phosphotyrosine binding motif termed immunotyrosine based activation motif ITAM 13 14 The larger CD79a isoform contains an insert in position 88 127 of human CD79a resulting in a complete immunoglobulin domain whereas the smaller isoform has only a truncated Ig like domain 5 CD79a has several cysteine residues one of which forms covalent bonds with CD79b 15 Function editCD79a plays multiple and diverse roles in B cell development and function The CD79a b heterodimer associates non covalently with the immunoglobulin heavy chain through its transmembrane region thus forming the BCR along with the immunoglobulin light chain and the pre BCR when associated with the surrogate light chain in developing B cells Association of the CD79a b heterodimer with the immunoglobulin heavy chain is required for surface expression of the BCR and BCR induced calcium flux and protein tyrosine phosphorylation 16 Genetic deletion of the transmembrane exon of CD79A results in loss of CD79a protein and a complete block of B cell development at the pro to pre B cell transition 17 Similarly humans with homozygous splice variants in CD79A predicted to result in loss of the transmembrane region and a truncated or absent protein display agammaglobulinemia and no peripheral B cells 7 18 19 The CD79a ITAM tyrosines human CD79a Tyr188 and Tyr199 mouse CD79a Tyr182 and Tyr193 phosphorylated in response to BCR crosslinking are critical for binding of Src homology 2 domain containing kinases such as spleen tyrosine kinase Syk and signal transduction by CD79a 20 21 In vivo the CD79a ITAM tyrosines synergize with the CD79b ITAM tyrosines to mediate the transition from the pro to the pre B cell stage as suggested by the analysis of mice with targeted mutations of the CD79a and CD79b ITAM 22 23 Loss of only one of the two functional CD79a b ITAMs resulted in impaired B cell development but B cell functions such as the T cell independent type II response and BCR mediated calcium flux in the available B cells were intact However the presence of both the CD79a and CD79b ITAM tyrosines were required for normal T cell dependent antibody responses 22 24 The CD79a cytoplasmic domain further contains a non ITAM tyrosine distal of the CD79a ITAM human CD79a Tyr210 mouse CD79a Tyr204 that can bind BLNK and Nck once phosphorylated 25 26 27 and is critical for BCR mediated B cell proliferation and B1 cell development 28 CD79a ITAM tyrosine phosphorylation and signaling is negatively regulated by serine and threonine residues in direct proximity of the ITAM human CD79a Ser197 Ser203 Thr209 mouse CD79a Ser191 Ser197 Thr203 29 30 and play a role in limiting formation of bone marrow plasma cells secreting IgG2a and IgG2b 23 Diagnostic relevance editThe CD79a protein is present on the surface of B cells throughout their life cycle and is absent on all other healthy cells making it a highly reliable marker for B cells in immunohistochemistry The protein remains present when B cells transform into active plasma cells and is also present in virtually all B cell neoplasms including B cell lymphomas plasmacytomas and myelomas It is also present in abnormal lymphocytes associated with some cases of Hodgkins disease Because even on B cell precursors it can be used to stain a wider range of cells than can the alternative B cell marker CD20 but the latter is more commonly retained on mature B cell lymphomas so that the two are often used together in immunohistochemistry panels 6 See also editCluster of differentiationReferences edit a b c GRCh38 Ensembl release 89 ENSG00000105369 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000003379 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b c d Entrez Gene CD79A CD79a molecule immunoglobulin associated alpha a b Anthony S Y L Cooper K Leong FJ 2003 Manual of Diagnostic Cytology 2 ed Greenwich Medical Media Ltd pp XX ISBN 1 84110 100 1 a b Online Mendelian Inheritance in Man OMIM 613501 Sakaguchi N Kashiwamura S Kimoto M Thalmann P Melchers F Nov 1988 B lymphocyte lineage restricted expression of mb 1 a gene with CD3 like structural properties The EMBO Journal 7 11 3457 64 doi 10 1002 j 1460 2075 1988 tb03220 x PMC 454845 PMID 2463161 Ha HJ Kubagawa H Burrows PD Mar 1992 Molecular cloning and expression pattern of a human gene homologous to the murine mb 1 gene Journal of Immunology 148 5 1526 31 doi 10 4049 jimmunol 148 5 1526 PMID 1538135 S2CID 22129592 Flaswinkel H Reth M 1992 Molecular cloning of the Ig alpha subunit of the human B cell antigen receptor complex Immunogenetics 36 4 266 9 doi 10 1007 bf00215058 PMID 1639443 S2CID 28622219 Sims R Vandergon VO Malone CS Mar 2012 The mouse B cell specific mb 1 gene encodes an immunoreceptor tyrosine based activation motif ITAM protein that may be evolutionarily conserved in diverse species by purifying selection Molecular Biology Reports 39 3 3185 96 doi 10 1007 s11033 011 1085 7 PMC 4667979 PMID 21688146 Flajnik MF Kasahara M Jan 2010 Origin and evolution of the adaptive immune system genetic events and selective pressures Nature Reviews Genetics 11 1 47 59 doi 10 1038 nrg2703 PMC 3805090 PMID 19997068 Reth M Mar 1989 Antigen receptor tail clue Nature 338 6214 383 4 Bibcode 1989Natur 338 383R doi 10 1038 338383b0 PMID 2927501 S2CID 5213145 Cambier JC Oct 1995 Antigen and Fc receptor signaling The awesome power of the immunoreceptor tyrosine based activation motif ITAM Journal of Immunology 155 7 3281 5 doi 10 4049 jimmunol 155 7 3281 PMID 7561018 S2CID 996547 Reth M 1992 Antigen receptors on B lymphocytes Annual Review of Immunology 10 1 97 121 doi 10 1146 annurev iy 10 040192 000525 PMID 1591006 Yang Jianying Reth Michael September 2010 Oligomeric organization of the B cell antigen receptor on resting cells Nature 467 7314 465 469 Bibcode 2010Natur 467 465Y doi 10 1038 nature09357 ISSN 1476 4687 PMID 20818374 S2CID 3261220 Pelanda R Braun U Hobeika E Nussenzweig MC Reth M Jul 2002 B cell progenitors are arrested in maturation but have intact VDJ recombination in the absence of Ig alpha and Ig beta Journal of Immunology 169 2 865 72 doi 10 4049 jimmunol 169 2 865 PMID 12097390 Minegishi Y Coustan Smith E Rapalus L Ersoy F Campana D Conley ME Oct 1999 Mutations in Igalpha CD79a result in a complete block in B cell development The Journal of Clinical Investigation 104 8 1115 21 doi 10 1172 JCI7696 PMC 408581 PMID 10525050 Wang Y Kanegane H Sanal O Tezcan I Ersoy F Futatani T Miyawaki T Apr 2002 Novel Igalpha CD79a gene mutation in a Turkish patient with B cell deficient agammaglobulinemia American Journal of Medical Genetics 108 4 333 6 doi 10 1002 ajmg 10296 PMID 11920841 Flaswinkel H Reth M Jan 1994 Dual role of the tyrosine activation motif of the Ig alpha protein during signal transduction via the B cell antigen receptor The EMBO Journal 13 1 83 9 doi 10 1002 j 1460 2075 1994 tb06237 x PMC 394781 PMID 8306975 Reth M Wienands J 1997 Initiation and processing of signals from the B cell antigen receptor Annual Review of Immunology 15 1 453 79 doi 10 1146 annurev immunol 15 1 453 PMID 9143696 a b Gazumyan A Reichlin A Nussenzweig MC Jul 2006 Ig beta tyrosine residues contribute to the control of B cell receptor signaling by regulating receptor internalization The Journal of Experimental Medicine 203 7 1785 94 doi 10 1084 jem 20060221 PMC 2118343 PMID 16818674 a b Patterson HC Kraus M Wang D Shahsafaei A Henderson JM Seagal J Otipoby KL Thai TH Rajewsky K Sep 2011 Cytoplasmic Ig alpha serine threonines fine tune Ig alpha tyrosine phosphorylation and limit bone marrow plasma cell formation Journal of Immunology 187 6 2853 8 doi 10 4049 jimmunol 1101143 PMC 3169759 PMID 21841126 Kraus M Pao LI Reichlin A Hu Y Canono B Cambier JC Nussenzweig MC Rajewsky K Aug 2001 Interference with immunoglobulin Ig alpha immunoreceptor tyrosine based activation motif ITAM phosphorylation modulates or blocks B cell development depending on the availability of an Igbeta cytoplasmic tail The Journal of Experimental Medicine 194 4 455 69 doi 10 1084 jem 194 4 455 PMC 2193498 PMID 11514602 Engels N Wollscheid B Wienands J Jul 2001 Association of SLP 65 BLNK with the B cell antigen receptor through a non ITAM tyrosine of Ig alpha European Journal of Immunology 31 7 2126 34 doi 10 1002 1521 4141 200107 31 7 lt 2126 aid immu2126 gt 3 0 co 2 o PMID 11449366 S2CID 31494726 Kabak S Skaggs BJ Gold MR Affolter M West KL Foster MS Siemasko K Chan AC Aebersold R Clark MR Apr 2002 The direct recruitment of BLNK to immunoglobulin alpha couples the B cell antigen receptor to distal signaling pathways Molecular and Cellular Biology 22 8 2524 35 doi 10 1128 MCB 22 8 2524 2535 2002 PMC 133735 PMID 11909947 Castello A Gaya M Tucholski J Oellerich T Lu KH Tafuri A Pawson T Wienands J Engelke M Batista FD Sep 2013 Nck mediated recruitment of BCAP to the BCR regulates the PI 3 K Akt pathway in B cells Nature Immunology 14 9 966 75 doi 10 1038 ni 2685 PMID 23913047 S2CID 2532325 Patterson HC Kraus M Kim YM Ploegh H Rajewsky K Jul 2006 The B cell receptor promotes B cell activation and proliferation through a non ITAM tyrosine in the Igalpha cytoplasmic domain Immunity 25 1 55 65 doi 10 1016 j immuni 2006 04 014 PMID 16860757 Muller R Wienands J Reth M Jul 2000 The serine and threonine residues in the Ig alpha cytoplasmic tail negatively regulate immunoreceptor tyrosine based activation motif mediated signal transduction Proceedings of the National Academy of Sciences of the United States of America 97 15 8451 4 Bibcode 2000PNAS 97 8451M doi 10 1073 pnas 97 15 8451 PMC 26968 PMID 10900006 Heizmann B Reth M Infantino S Oct 2010 Syk is a dual specificity kinase that self regulates the signal output from the B cell antigen receptor Proceedings of the National Academy of Sciences of the United States of America 107 43 18563 8 Bibcode 2010PNAS 10718563H doi 10 1073 pnas 1009048107 PMC 2972992 PMID 20940318 Further reading editHerren B Burrows PD 2003 B cell restricted human mb 1 gene expression function and lineage infidelity Immunologic Research 26 1 3 35 43 doi 10 1385 IR 26 1 3 035 PMID 12403343 S2CID 38456117 Leduc I Preud homme JL Cogne M Oct 1992 Structure and expression of the mb 1 transcript in human lymphoid cells Clinical and Experimental Immunology 90 1 141 6 doi 10 1111 j 1365 2249 1992 tb05846 x PMC 1554548 PMID 1395095 Muller B Cooper L Terhorst C Jun 1992 Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin associated protein B29 European Journal of Immunology 22 6 1621 5 doi 10 1002 eji 1830220641 PMID 1534761 S2CID 23910309 Hutchcroft JE Harrison ML Geahlen RL Apr 1992 Association of the 72 kDa protein tyrosine kinase PTK72 with the B cell antigen receptor The Journal of Biological Chemistry 267 12 8613 9 doi 10 1016 S0021 9258 18 42487 8 PMID 1569106 Yu LM Chang TW Jan 1992 Human mb 1 gene complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes Journal of Immunology 148 2 633 7 doi 10 4049 jimmunol 148 2 633 PMID 1729378 S2CID 24075079 Venkitaraman AR Williams GT Dariavach P Neuberger MS Aug 1991 The B cell antigen receptor of the five immunoglobulin classes Nature 352 6338 777 81 Bibcode 1991Natur 352 777V doi 10 1038 352777a0 PMID 1881434 S2CID 4246284 Kurosaki T Johnson SA Pao L Sada K Yamamura H Cambier JC Dec 1995 Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling The Journal of Experimental Medicine 182 6 1815 23 doi 10 1084 jem 182 6 1815 PMC 2192262 PMID 7500027 Lankester AC van Schijndel GM Cordell JL van Noesel CJ van Lier RA Apr 1994 CD5 is associated with the human B cell antigen receptor complex European Journal of Immunology 24 4 812 6 doi 10 1002 eji 1830240406 PMID 7512031 S2CID 25093082 Vasile S Coligan JE Yoshida M Seon BK Apr 1994 Isolation and chemical characterization of the human B29 and mb 1 proteins of the B cell antigen receptor complex Molecular Immunology 31 6 419 27 doi 10 1016 0161 5890 94 90061 2 PMID 7514267 Brown VK Ogle EW Burkhardt AL Rowley RB Bolen JB Justement LB Jun 1994 Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase CD45 The Journal of Biological Chemistry 269 25 17238 44 doi 10 1016 S0021 9258 17 32545 0 PMID 7516335 Pani G Kozlowski M Cambier JC Mills GB Siminovitch KA Jun 1995 Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor associated protein involved in the regulation of B cell signaling The Journal of Experimental Medicine 181 6 2077 84 doi 10 1084 jem 181 6 2077 PMC 2192043 PMID 7539038 External links editCD79A protein human at the U S National Library of Medicine Medical Subject Headings MeSH Human CD79A genome location and CD79A gene details page in the UCSC Genome Browser This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title CD79A amp oldid 1169973744, wikipedia, wiki, book, books, library,

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