Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta, and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues.
While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is composed of two distinct domains.
The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Various adducin beta mRNAs, alternatively spliced at 3' end and/or internally spliced and encoding different isoforms, have been described. The functions of all the different isoforms are not known.[6]
^ abcGRCh38: Ensembl release 89: ENSG00000075340 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000030000 - 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.
^Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V (Nov 1991). "Primary structure and domain organization of human alpha and beta adducin". J Cell Biol. 115 (3): 665–75. doi:10.1083/jcb.115.3.665. PMC2289184. PMID 1840603.
^Shima T, Okumura N, Takao T, Satomi Y, Yagi T, Okada M, Nagai K (November 2001). "Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin". J. Biol. Chem. 276 (45): 42233–40. doi:10.1074/jbc.M102699200. PMID 11526103.
External linksedit
Human ADD2 genome location and ADD2 gene details page in the UCSC Genome Browser.
Further readingedit
Gilligan DM, Lieman J, Bennett V (1996). "Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization". Genomics. 28 (3): 610–2. doi:10.1006/geno.1995.1205. PMID 7490111.
Hughes CA, Bennett V (1995). "Adducin: a physical model with implications for function in assembly of spectrin-actin complexes". J. Biol. Chem. 270 (32): 18990–6. doi:10.1074/jbc.270.32.18990. PMID 7642559.
Miyazaki M, Kaibuchi K, Shirataki H, et al. (1995). "Rabphilin-3A binds to a M(r) 115,000 polypeptide in a phosphatidylserine- and Ca(2+)-dependent manner". Brain Res. Mol. Brain Res. 28 (1): 29–36. doi:10.1016/0169-328X(94)00180-M. PMID 7707875.
Miyazaki M, Shirataki H, Kohno H, et al. (1995). "Identification as beta-adducin of a protein interacting with rabphilin-3A in the presence of Ca2+ and phosphatidylserine". Biochem. Biophys. Res. Commun. 205 (1): 460–6. doi:10.1006/bbrc.1994.2688. PMID 7999065.
White RA, Angeloni SV, Pasztor LM (1996). "Chromosomal localization of the beta-adducin gene to mouse chromosome 6 and human chromosome 2". Mamm. Genome. 6 (10): 741–3. doi:10.1007/BF00354298. PMID 8563174. S2CID 23628451.
Tisminetzky S, Devescovi G, Tripodi G, et al. (1996). "Genomic organisation and chromosomal localisation of the gene encoding human beta adducin". Gene. 167 (1–2): 313–6. doi:10.1016/0378-1119(95)00591-9. PMID 8566798.
Matsuoka Y, Hughes CA, Bennett V (1996). "Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C". J. Biol. Chem. 271 (41): 25157–66. doi:10.1074/jbc.271.41.25157. PMID 8810272.
Gilligan DM, Lozovatsky L, Silberfein A (1997). "Organization of the human beta-adducin gene (ADD2)". Genomics. 43 (2): 141–8. doi:10.1006/geno.1997.4802. PMID 9244430.
Matsuoka Y, Li X, Bennett V (1998). "Adducin Is an In Vivo Substrate for Protein Kinase C: Phosphorylation in the MARCKS-related Domain Inhibits Activity in Promoting Spectrin–Actin Complexes and Occurs in Many Cells, Including Dendritic Spines of Neurons". J. Cell Biol. 142 (2): 485–97. doi:10.1083/jcb.142.2.485. PMC2133059. PMID 9679146.
Gilligan DM, Lozovatsky L, Gwynn B, et al. (1999). "Targeted disruption of the β adducin gene (Add2) causes red blood cell spherocytosis in mice". Proc. Natl. Acad. Sci. U.S.A. 96 (19): 10717–22. Bibcode:1999PNAS...9610717G. doi:10.1073/pnas.96.19.10717. PMC17949. PMID 10485892.
Shima T, Okumura N, Takao T, et al. (2001). "Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin". J. Biol. Chem. 276 (45): 42233–40. doi:10.1074/jbc.M102699200. PMID 11526103.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Citterio L, Tizzoni L, Catalano M, et al. (2003). "Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants". Biochem. Biophys. Res. Commun. 309 (2): 359–67. doi:10.1016/j.bbrc.2003.08.011. PMID 12951058.
Tikhonoff V, Kuznetsova T, Stolarz K, et al. (2004). "beta-Adducin polymorphisms, blood pressure, and sodium excretion in three European populations". Am. J. Hypertens. 16 (10): 840–6. doi:10.1016/S0895-7061(03)00975-0. PMID 14553963.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Efendiev R, Krmar RT, Ogimoto G, et al. (2005). "Hypertension-linked mutation in the adducin alpha-subunit leads to higher AP2-mu2 phosphorylation and impaired Na+,K+-ATPase trafficking in response to GPCR signals and intracellular sodium". Circ. Res. 95 (11): 1100–8. doi:10.1161/01.RES.0000149570.20845.89. PMID 15528469.
Lanzani C, Citterio L, Jankaricova M, et al. (2005). "Role of the adducin family genes in human essential hypertension". J. Hypertens. 23 (3): 543–9. doi:10.1097/01.hjh.0000160210.48479.78. PMID 15716695. S2CID 37253591.
This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.
add2, graphics, expansion, card, system, sdvo, beta, adducin, protein, that, humans, encoded, gene, identifiersaliases, addb, adducin, 2external, idsomim, 102681, 87919, homologene, 1221, genecards, gene, location, human, chromosome, human, band2p13, 3start70,. For the ADD2 graphics expansion card system see SDVO Beta adducin is a protein that in humans is encoded by the ADD2 gene 5 6 ADD2IdentifiersAliasesADD2 ADDB adducin 2External IDsOMIM 102681 MGI 87919 HomoloGene 1221 GeneCards ADD2Gene location Human Chr Chromosome 2 human 1 Band2p13 3Start70 607 618 bp 1 End70 768 225 bp 1 Gene location Mouse Chr Chromosome 6 mouse 2 Band6 C3 D1 6 37 55 cMStart86 005 663 bp 2 End86 101 391 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inBrodmann area 10middle temporal gyrusBrodmann area 23frontal poleRegion I of hippocampus properpostcentral gyrusBrodmann area 46entorhinal cortexsuperior frontal gyrusorbitofrontal cortexTop expressed inolfactory tubercleRegion I of hippocampus properpiriform cortexdentate gyrusfacial motor nucleussubiculumpontine nucleivisual cortexprimary motor cortexnucleus accumbensMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionspectrin binding protein homodimerization activity structural molecule activity calmodulin binding actin filament binding protein heterodimerization activity actin binding protein kinase bindingCellular componentF actin capping protein complex cytoplasm cytosol membrane plasma membrane cytoskeleton postsynaptic density cytoplasmic vesicle plasma membrane raftBiological processbarbed end actin filament capping actin filament bundle assembly transmembrane transport positive regulation of protein binding actin cytoskeleton organization leukocyte migration leukocyte tethering or rolling protein containing complex assembly hemopoiesis synapse assemblySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez11911519EnsemblENSG00000075340ENSMUSG00000030000UniProtP35612Q9QYB8RefSeq mRNA NM 001185054NM 001185055NM 001617NM 017482NM 017483NM 017484NM 017485NM 017486NM 017487NM 017488NM 001271857NM 001271858NM 001271859NM 001271860NM 001271861NM 013458RefSeq protein NP 001171983NP 001171984NP 001608NP 059516NP 059522NP 001258786NP 001258787NP 001258788NP 001258789NP 001258790NP 038486Location UCSC Chr 2 70 61 70 77 MbChr 6 86 01 86 1 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 References 4 External links 5 Further readingFunction editAdducins are heteromeric proteins composed of different subunits referred to as adducin alpha beta and gamma The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin actin network in erythrocytes and at sites of cell cell contact in epithelial tissues While adducins alpha and gamma are ubiquitously expressed the expression of adducin beta is restricted to brain and hematopoietic tissues Adducin originally purified from human erythrocytes was found to be a heterodimer of adducins alpha and beta Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension Heterodimers consisting of alpha and gamma subunits have also been described Structurally each subunit is composed of two distinct domains The amino terminal region is protease resistant and globular in shape while the carboxy terminal region is protease sensitive The latter contains multiple phosphorylation sites for protein kinase C the binding site for calmodulin and is required for association with spectrin and actin Various adducin beta mRNAs alternatively spliced at 3 end and or internally spliced and encoding different isoforms have been described The functions of all the different isoforms are not known 6 Interactions editADD2 has been shown to interact with FYN 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000075340 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000030000 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 Joshi R Gilligan DM Otto E McLaughlin T Bennett V Nov 1991 Primary structure and domain organization of human alpha and beta adducin J Cell Biol 115 3 665 75 doi 10 1083 jcb 115 3 665 PMC 2289184 PMID 1840603 a b Entrez Gene ADD2 adducin 2 beta Shima T Okumura N Takao T Satomi Y Yagi T Okada M Nagai K November 2001 Interaction of the SH2 domain of Fyn with a cytoskeletal protein beta adducin J Biol Chem 276 45 42233 40 doi 10 1074 jbc M102699200 PMID 11526103 External links editHuman ADD2 genome location and ADD2 gene details page in the UCSC Genome Browser Further reading editGilligan DM Lieman J Bennett V 1996 Assignment of the human beta adducin gene ADD2 to 2p13 p14 by in situ hybridization Genomics 28 3 610 2 doi 10 1006 geno 1995 1205 PMID 7490111 Hughes CA Bennett V 1995 Adducin a physical model with implications for function in assembly of spectrin actin complexes J Biol Chem 270 32 18990 6 doi 10 1074 jbc 270 32 18990 PMID 7642559 Miyazaki M Kaibuchi K Shirataki H et al 1995 Rabphilin 3A binds to a M r 115 000 polypeptide in a phosphatidylserine and Ca 2 dependent manner Brain Res Mol Brain Res 28 1 29 36 doi 10 1016 0169 328X 94 00180 M PMID 7707875 Miyazaki M Shirataki H Kohno H et al 1995 Identification as beta adducin of a protein interacting with rabphilin 3A in the presence of Ca2 and phosphatidylserine Biochem Biophys Res Commun 205 1 460 6 doi 10 1006 bbrc 1994 2688 PMID 7999065 White RA Angeloni SV Pasztor LM 1996 Chromosomal localization of the beta adducin gene to mouse chromosome 6 and human chromosome 2 Mamm Genome 6 10 741 3 doi 10 1007 BF00354298 PMID 8563174 S2CID 23628451 Tisminetzky S Devescovi G Tripodi G et al 1996 Genomic organisation and chromosomal localisation of the gene encoding human beta adducin Gene 167 1 2 313 6 doi 10 1016 0378 1119 95 00591 9 PMID 8566798 Matsuoka Y Hughes CA Bennett V 1996 Adducin regulation Definition of the calmodulin binding domain and sites of phosphorylation by protein kinases A and C J Biol Chem 271 41 25157 66 doi 10 1074 jbc 271 41 25157 PMID 8810272 Gilligan DM Lozovatsky L Silberfein A 1997 Organization of the human beta adducin gene ADD2 Genomics 43 2 141 8 doi 10 1006 geno 1997 4802 PMID 9244430 Matsuoka Y Li X Bennett V 1998 Adducin Is an In Vivo Substrate for Protein Kinase C Phosphorylation in the MARCKS related Domain Inhibits Activity in Promoting Spectrin Actin Complexes and Occurs in Many Cells Including Dendritic Spines of Neurons J Cell Biol 142 2 485 97 doi 10 1083 jcb 142 2 485 PMC 2133059 PMID 9679146 Gilligan DM Lozovatsky L Gwynn B et al 1999 Targeted disruption of the b adducin gene Add2 causes red blood cell spherocytosis in mice Proc Natl Acad Sci U S A 96 19 10717 22 Bibcode 1999PNAS 9610717G doi 10 1073 pnas 96 19 10717 PMC 17949 PMID 10485892 Shima T Okumura N Takao T et al 2001 Interaction of the SH2 domain of Fyn with a cytoskeletal protein beta adducin J Biol Chem 276 45 42233 40 doi 10 1074 jbc M102699200 PMID 11526103 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Citterio L Tizzoni L Catalano M et al 2003 Expression analysis of the human adducin gene family and evidence of ADD2 beta4 multiple splicing variants Biochem Biophys Res Commun 309 2 359 67 doi 10 1016 j bbrc 2003 08 011 PMID 12951058 Tikhonoff V Kuznetsova T Stolarz K et al 2004 beta Adducin polymorphisms blood pressure and sodium excretion in three European populations Am J Hypertens 16 10 840 6 doi 10 1016 S0895 7061 03 00975 0 PMID 14553963 Brandenberger R Wei H Zhang S et al 2005 Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation Nat Biotechnol 22 6 707 16 doi 10 1038 nbt971 PMID 15146197 S2CID 27764390 Ballif BA Villen J Beausoleil SA et al 2005 Phosphoproteomic analysis of the developing mouse brain Mol Cell Proteomics 3 11 1093 101 doi 10 1074 mcp M400085 MCP200 PMID 15345747 Gerhard DS Wagner L Feingold EA et al 2004 The Status Quality and Expansion of the NIH Full Length cDNA Project The Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Efendiev R Krmar RT Ogimoto G et al 2005 Hypertension linked mutation in the adducin alpha subunit leads to higher AP2 mu2 phosphorylation and impaired Na K ATPase trafficking in response to GPCR signals and intracellular sodium Circ Res 95 11 1100 8 doi 10 1161 01 RES 0000149570 20845 89 PMID 15528469 Lanzani C Citterio L Jankaricova M et al 2005 Role of the adducin family genes in human essential hypertension J Hypertens 23 3 543 9 doi 10 1097 01 hjh 0000160210 48479 78 PMID 15716695 S2CID 37253591 nbsp This article on a gene on human chromosome 2 is a stub You can help Wikipedia by expanding it vte Retrieved from https en 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