Tubulin alpha-1A chain is an alpha-tubulin that participates in the formation of microtubules - structural proteins that participate in cytoskeletal structure. Specifically, microtubules are composed of a heterodimer of alpha and beta-tubulin molecules. Cowan et al. demonstrated that bα1 is a primary α-tubulin of the human fetal brain, and that it is expressed solely in that structure, by way of Northern blot.[8] Miller et al. further elaborated on the role of α-tubulins and the process of neuronal development and maturation, comparing the expressions of rat α-tubulins Tα1 and T26. These two rat α-tubulins are homologs of bα1 and kα1 showing that a rat homolog of human TUBA1A (Tα1) had elevated expression during the extension of neuronal processes. Culturing of pheochromocytoma cells with Nerve Growth Factor (NGF) induced differentiation and the development of neuronal processes. Northern blot assay showed markedly elevated levels of Tα1 mRNA expression; T26 mRNA expression increased minimally with exposure to NGF.[9] These data suggest that TUBA1A models the brain by participating in the directing of neuronal migration through the ability of microtubules to readily form and break polymers to extend and retract processes to induce nucleokinesis.[10] Poirier et al. used RNA in situ hybridization to show TUBA1A expression in mice embryo; embryo sections from embryonic day 16.5 “showed a strong labeling in the telencephalon, diencephalon, and mesencephalon, the developing cerebellum, the brainstem, the spinal cord, and the dorsal root ganglia”.[11]
Function
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to mouse and rat Tuba1 gene. Northern blotting studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q.[7]
Mutations to the TUBA1A gene manifest clinically as Type 3 Lissencephaly. In general, lissencephaly is characterized by agyria (lacking of gyri and sulci to the brain – a smooth brain), seizure activity, failure to thrive, as well as intellectual disability and psychomotor retardation, often to a profound degree.[11] The symptoms of Lis3 Lissencephaly are not especially different from generalized lissencephaly (Lis1, related to PAFAH1B1). Diagnosis of lissencephaly generally is made from the symptom profile, while attribution to a specific type is obtained by microarray. Treatment is symptomatic; anti-convulsive drugs for seizure activity, g-button gastrostomy to feed the child, physical therapy for muscle disorders. TUBA1A mutation is common in microlissencephaly
Animal model
Keays et al. describe a mouse with a mutation of the TUBA1A gene induced by N-ethyl-N-nitrosourea. The relevant point mutation resulted in S140G;[13] the site of the mutation participates in the N-site of the formed α-tubulin, and participates in stabilizing the α-β tubulin polymer by binding GTP at this site.[14] The S140G mutation resulted in the formation of a “compromised GTP binding pocket”. Authors note defects associated with cortical layers II/III and IV, especially in cortical neuronal migration (with respect to wild-type counterparts), showing that the S140G mutation has value as a model for detailing disease associated with the Human TUBA homolog.[13]
References
^ abcGRCh38: Ensembl release 89: ENSG00000167552 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000072235 - 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.
^Crabtree DV, Ojima I, Geng X, Adler AJ (August 2001). "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site". Bioorganic & Medicinal Chemistry. 9 (8): 1967–76. doi:10.1016/S0968-0896(01)00103-1. PMID 11504633.
^Hall JL, Cowan NJ (January 1985). "Structural features and restricted expression of a human alpha-tubulin gene". Nucleic Acids Research. 13 (1): 207–23. doi:10.1093/nar/13.1.207. PMC340985. PMID 3839072.
^Cowan, N. J.; Dobner, P. R.; Fuchs, E. V.; Cleveland, D. W. (1983). "Expression of Human α-Tubulin Genes: Interspecies Conversion of 3' Untranslated Regions". Molecular and Cellular Biology. 3 (10): 1738–1739, 1742. doi:10.1128/mcb.3.10.1738. PMC370035. PMID 6646120.
^Mill, F. D.; Naus, C. C.; Durand, M.; Bloom, F. E.; Milner, R. J. (1987). "Isotypes of alpha-tubulin are differentially regulated during neuronal maturation". The Journal of Cell Biology. 105 (6): 3065–3073. doi:10.1083/jcb.105.6.3065. PMC2114727. PMID 3693406.
^Sakakaibara, A.; Ando, R.; Spair, T.; Tanaka, T. (July 2013). "Microtubule dynamics in neuronal morphogenesis". Open Biology. 3 (7): 130061. doi:10.1098/rsob.130061. PMC3728923. PMID 23864552.
^ abPoirier, K.; Keays, D. A.; Francis, F.; Saillour, Y.; Bahi, N.; Manouvrier, S.; Fallet-Bianco, C.; Paquier, L.; Toutain, A.; Tuy, F. P. D.; Bienvenu, T.; Joriot, S.; Odent, S.; Ville, D.; Desguerre, I.; Goldenberg, A.; Moutard, M.-L.; Fryns, J.-P.; van Esch, H.; Harvey, R. J.; Siebold, C.; Flint, J.; Beldjord, C.; Chelly, J. (November 2007). "Large Spectrum of Lissencephaly and Pachygyria Phenotypes Resulting from De Novo Missense Mutations in Tubulin Alpha 1A (TUBA1A)". Human Mutation. 28 (11): 1058–1061. doi:10.1002/humu.20572. PMID 17584854. S2CID 22681290.
^Sapir T, Elbaum M, Reiner O (December 1997). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit". The EMBO Journal. 16 (23): 6977–84. doi:10.1093/emboj/16.23.6977. PMC1170301. PMID 9384577.
^ abKeays, D. A.; Tian, G.; Poirier, K.; Huang, G.-J.; Siebold, C.; Cleak, J.; Oliver, P. L.; Fray, M.; Harvey, R. J.; Molnár, Z.; Piñon, M. C.; Dear, N.; Valdar, W.; Brown, S. D.; Davies, K. E.; Rawlins, J. N. P.; Cowan, N. J.; Nolan, P.; Chelly, J.; Flint, J. (January 2007). "Mutations in α-Tubulin Cause Abnormal Neuronal Migration in Mice and Lissencephaly in Humans". Cell. 128 (1): 45–46, 48–50. doi:10.1016/j.cell.2006.12.017. PMC1885944. PMID 17218254.
^Löwe, J.; Li, H.; Downing, K. H.; Nogales, E. (November 2001). "Refined structure of αβ-tubulin at 3.5 Å resolution". Journal of Molecular Biology. 313 (5): 1045–1046. doi:10.1006/jmbi.2001.5077. PMID 11700061.
Further reading
Desai A, Mitchison TJ (July 1998). "Tubulin and FtsZ structures: functional and therapeutic implications". BioEssays. 20 (7): 523–7. doi:10.1002/(SICI)1521-1878(199807)20:7<523::AID-BIES1>3.0.CO;2-L. PMID 9722999.
Oakley BR (December 2000). "An abundance of tubulins". Trends in Cell Biology. 10 (12): 537–42. doi:10.1016/S0962-8924(00)01857-2. PMID 11121746.
Dutcher SK (February 2001). "The tubulin fraternity: alpha to eta". Current Opinion in Cell Biology. 13 (1): 49–54. doi:10.1016/S0955-0674(00)00173-3. PMID 11163133.
Miller FD, Naus CC, Durand M, Bloom FE, Milner RJ (December 1987). "Isotypes of alpha-tubulin are differentially regulated during neuronal maturation". The Journal of Cell Biology. 105 (6 Pt 2): 3065–73. doi:10.1083/jcb.105.6.3065. PMC2114727. PMID 3693406.
Cowan NJ, Dobner PR, Fuchs EV, Cleveland DW (October 1983). "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions". Molecular and Cellular Biology. 3 (10): 1738–45. doi:10.1128/mcb.3.10.1738. PMC370035. PMID 6646120.
Alexandrova N, Niklinski J, Bliskovsky V, Otterson GA, Blake M, Kaye FJ, Zajac-Kaye M (September 1995). "The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro". Molecular and Cellular Biology. 15 (9): 5188–95. doi:10.1128/MCB.15.9.5188. PMC230766. PMID 7651436.
Sapir T, Elbaum M, Reiner O (December 1997). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit". The EMBO Journal. 16 (23): 6977–84. doi:10.1093/emboj/16.23.6977. PMC1170301. PMID 9384577.
Kinnunen T, Kaksonen M, Saarinen J, Kalkkinen N, Peng HB, Rauvala H (April 1998). "Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth". The Journal of Biological Chemistry. 273 (17): 10702–8. doi:10.1074/jbc.273.17.10702. PMID 9553134.
Faruki S, Geahlen RL, Asai DJ (July 2000). "Syk-dependent phosphorylation of microtubules in activated B-lymphocytes". Journal of Cell Science. 113 (14): 2557–65. doi:10.1242/jcs.113.14.2557. PMID 10862713.
Watts NR, Sackett DL, Ward RD, Miller MW, Wingfield PT, Stahl SS, Steven AC (July 2000). "HIV-1 rev depolymerizes microtubules to form stable bilayered rings". The Journal of Cell Biology. 150 (2): 349–60. doi:10.1083/jcb.150.2.349. PMC2180222. PMID 10908577.
Germani A, Bruzzoni-Giovanelli H, Fellous A, Gisselbrecht S, Varin-Blank N, Calvo F (December 2000). "SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis". Oncogene. 19 (52): 5997–6006. doi:10.1038/sj.onc.1204002. PMID 11146551.
Payton JE, Perrin RJ, Clayton DF, George JM (November 2001). "Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells". Brain Research. Molecular Brain Research. 95 (1–2): 138–45. doi:10.1016/S0169-328X(01)00257-1. PMID 11687285.
Bifulco M, Laezza C, Stingo S, Wolff J (February 2002). "2',3'-Cyclic nucleotide 3'-phosphodiesterase: a membrane-bound, microtubule-associated protein and membrane anchor for tubulin". Proceedings of the National Academy of Sciences of the United States of America. 99 (4): 1807–12. Bibcode:2002PNAS...99.1807B. doi:10.1073/pnas.042678799. PMC122275. PMID 11842207.
Saugstad JA, Yang S, Pohl J, Hall RA, Conn PJ (March 2002). "Interaction between metabotropic glutamate receptor 7 and alpha tubulin". Journal of Neurochemistry. 80 (6): 980–8. doi:10.1046/j.0022-3042.2002.00778.x. PMC2925652. PMID 11953448.
Ivings L, Pennington SR, Jenkins R, Weiss JL, Burgoyne RD (May 2002). "Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin". The Biochemical Journal. 363 (Pt 3): 599–608. doi:10.1042/0264-6021:3630599. PMC1222513. PMID 11964161.
External links
Overview of all the structural information available in the PDB for UniProt: Q71U36 (Human Tubulin alpha-1A chain) at the PDBe-KB.
Overview of all the structural information available in the PDB for UniProt: P68369 (Mouse Tubulin alpha-1A chain) at the PDBe-KB.
January 31, 2023
tubulin, alpha, chain, protein, that, humans, encoded, tuba1a, gene, tuba1aavailable, structurespdbortholog, search, pdbe, rcsblist, codes3hkc, 4x20, 3hke, 3n2g, 4x1y, 3n2k, 4x1i, 4x1k, 3hkb, 3hkd, 5jcoidentifiersaliasestuba1a, alpha, lis3, tuba3, tubulin, alp. Tubulin alpha 1A chain is a protein that in humans is encoded by the TUBA1A gene 5 6 7 TUBA1AAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes3HKC 4X20 3HKE 3N2G 4X1Y 3N2K 4X1I 4X1K 3HKB 3HKD 5JCOIdentifiersAliasesTUBA1A B ALPHA 1 LIS3 TUBA3 tubulin alpha 1aExternal IDsOMIM 602529 MGI 98869 HomoloGene 68498 GeneCards TUBA1AGene location Human Chr Chromosome 12 human 1 Band12q13 12Start49 184 686 bp 1 End49 189 080 bp 1 Gene location Mouse Chr Chromosome 15 mouse 2 Band15 F1 15 55 29 cMStart98 847 718 bp 2 End98 851 584 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inendothelial cellganglionic eminenceinferior ganglion of vagus nervesuperior vestibular nucleusspinal gangliainferior olivary nucleusbronchial epithelial celloptic nervesubthalamic nucleusBrodmann area 23Top expressed intrigeminal ganglionmammillary bodymedial dorsal nucleusfossacondylemedial vestibular nucleusmedian eminencesuperior cervical ganglionmedial geniculate nucleusparaventricular nucleus of hypothalamusMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding protein domain specific binding GTP binding structural molecule activity structural constituent of cytoskeleton protein binding GTPase activityCellular componentcytoplasm recycling endosome cytosol myelin sheath cytoplasmic microtubule cytoplasmic ribonucleoprotein granule microtubule extracellular exosome cytoskeleton nucleus microtubule cytoskeleton membrane raft neuromuscular junctionBiological processcytoskeleton dependent intracellular transport cell division G2 M transition of mitotic cell cycle microtubule based process cytoskeleton organization ciliary basal body plasma membrane docking regulation of G2 M transition of mitotic cell cycle microtubule cytoskeleton organization mitotic cell cycle regulation of synapse organizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez784622142EnsemblENSG00000167552ENSMUSG00000072235UniProtQ71U36P68369RefSeq mRNA NM 006009NM 001270399NM 001270400NM 011653RefSeq protein NP 001257328NP 001257329NP 006000NP 035783Location UCSC Chr 12 49 18 49 19 MbChr 15 98 85 98 85 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Background 2 Function 3 Interactions 4 Disease 5 Animal model 6 References 7 Further reading 8 External linksBackground EditTubulin alpha 1A chain is an alpha tubulin that participates in the formation of microtubules structural proteins that participate in cytoskeletal structure Specifically microtubules are composed of a heterodimer of alpha and beta tubulin molecules Cowan et al demonstrated that ba1 is a primary a tubulin of the human fetal brain and that it is expressed solely in that structure by way of Northern blot 8 Miller et al further elaborated on the role of a tubulins and the process of neuronal development and maturation comparing the expressions of rat a tubulins Ta1 and T26 These two rat a tubulins are homologs of ba1 and ka1 showing that a rat homolog of human TUBA1A Ta1 had elevated expression during the extension of neuronal processes Culturing of pheochromocytoma cells with Nerve Growth Factor NGF induced differentiation and the development of neuronal processes Northern blot assay showed markedly elevated levels of Ta1 mRNA expression T26 mRNA expression increased minimally with exposure to NGF 9 These data suggest that TUBA1A models the brain by participating in the directing of neuronal migration through the ability of microtubules to readily form and break polymers to extend and retract processes to induce nucleokinesis 10 Poirier et al used RNA in situ hybridization to show TUBA1A expression in mice embryo embryo sections from embryonic day 16 5 showed a strong labeling in the telencephalon diencephalon and mesencephalon the developing cerebellum the brainstem the spinal cord and the dorsal root ganglia 11 Function EditMicrotubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins The genes encoding these microtubule constituents belong to the tubulin superfamily which is composed of six distinct families Genes from the alpha beta and gamma tubulin families are found in all eukaryotes The alpha and beta tubulins represent the major components of microtubules while gamma tubulin plays a critical role in the nucleation of microtubule assembly There are multiple alpha and beta tubulin genes which are highly conserved among species This gene encodes alpha tubulin and is highly similar to mouse and rat Tuba1 gene Northern blotting studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells This gene is one of three alpha tubulin genes in a cluster on chromosome 12q 7 Interactions EditTUBA1A has been shown to interact with PAFAH1B1 12 Disease EditMutations to the TUBA1A gene manifest clinically as Type 3 Lissencephaly In general lissencephaly is characterized by agyria lacking of gyri and sulci to the brain a smooth brain seizure activity failure to thrive as well as intellectual disability and psychomotor retardation often to a profound degree 11 The symptoms of Lis3 Lissencephaly are not especially different from generalized lissencephaly Lis1 related to PAFAH1B1 Diagnosis of lissencephaly generally is made from the symptom profile while attribution to a specific type is obtained by microarray Treatment is symptomatic anti convulsive drugs for seizure activity g button gastrostomy to feed the child physical therapy for muscle disorders TUBA1A mutation is common in microlissencephalyAnimal model EditKeays et al describe a mouse with a mutation of the TUBA1A gene induced by N ethyl N nitrosourea The relevant point mutation resulted in S140G 13 the site of the mutation participates in the N site of the formed a tubulin and participates in stabilizing the a b tubulin polymer by binding GTP at this site 14 The S140G mutation resulted in the formation of a compromised GTP binding pocket Authors note defects associated with cortical layers II III and IV especially in cortical neuronal migration with respect to wild type counterparts showing that the S140G mutation has value as a model for detailing disease associated with the Human TUBA homolog 13 References Edit a b c GRCh38 Ensembl release 89 ENSG00000167552 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000072235 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 Crabtree DV Ojima I Geng X Adler AJ August 2001 Tubulins in the primate retina evidence that xanthophylls may be endogenous ligands for the paclitaxel binding site Bioorganic amp Medicinal Chemistry 9 8 1967 76 doi 10 1016 S0968 0896 01 00103 1 PMID 11504633 Hall JL Cowan NJ January 1985 Structural features and restricted expression of a human alpha tubulin gene Nucleic Acids Research 13 1 207 23 doi 10 1093 nar 13 1 207 PMC 340985 PMID 3839072 a b Entrez Gene TUBA1A tubulin alpha 1a Cowan N J Dobner P R Fuchs E V Cleveland D W 1983 Expression of Human a Tubulin Genes Interspecies Conversion of 3 Untranslated Regions Molecular and Cellular Biology 3 10 1738 1739 1742 doi 10 1128 mcb 3 10 1738 PMC 370035 PMID 6646120 Mill F D Naus C C Durand M Bloom F E Milner R J 1987 Isotypes of alpha tubulin are differentially regulated during neuronal maturation The Journal of Cell Biology 105 6 3065 3073 doi 10 1083 jcb 105 6 3065 PMC 2114727 PMID 3693406 Sakakaibara A Ando R Spair T Tanaka T July 2013 Microtubule dynamics in neuronal morphogenesis Open Biology 3 7 130061 doi 10 1098 rsob 130061 PMC 3728923 PMID 23864552 a b Poirier K Keays D A Francis F Saillour Y Bahi N Manouvrier S Fallet Bianco C Paquier L Toutain A Tuy F P D Bienvenu T Joriot S Odent S Ville D Desguerre I Goldenberg A Moutard M L Fryns J P van Esch H Harvey R J Siebold C Flint J Beldjord C Chelly J November 2007 Large Spectrum of Lissencephaly and Pachygyria Phenotypes Resulting from De Novo Missense Mutations in Tubulin Alpha 1A TUBA1A Human Mutation 28 11 1058 1061 doi 10 1002 humu 20572 PMID 17584854 S2CID 22681290 Sapir T Elbaum M Reiner O December 1997 Reduction of microtubule catastrophe events by LIS1 platelet activating factor acetylhydrolase subunit The EMBO Journal 16 23 6977 84 doi 10 1093 emboj 16 23 6977 PMC 1170301 PMID 9384577 a b Keays D A Tian G Poirier K Huang G J Siebold C Cleak J Oliver P L Fray M Harvey R J Molnar Z Pinon M C Dear N Valdar W Brown S D Davies K E Rawlins J N P Cowan N J Nolan P Chelly J Flint J January 2007 Mutations in a Tubulin Cause Abnormal Neuronal Migration in Mice and Lissencephaly in Humans Cell 128 1 45 46 48 50 doi 10 1016 j cell 2006 12 017 PMC 1885944 PMID 17218254 Lowe J Li H Downing K H Nogales E November 2001 Refined structure of ab tubulin at 3 5 A resolution Journal of Molecular Biology 313 5 1045 1046 doi 10 1006 jmbi 2001 5077 PMID 11700061 Further reading EditDesai A Mitchison TJ July 1998 Tubulin and FtsZ structures functional and therapeutic implications BioEssays 20 7 523 7 doi 10 1002 SICI 1521 1878 199807 20 7 lt 523 AID BIES1 gt 3 0 CO 2 L PMID 9722999 Oakley BR December 2000 An abundance of tubulins Trends in Cell Biology 10 12 537 42 doi 10 1016 S0962 8924 00 01857 2 PMID 11121746 Dutcher SK February 2001 The tubulin fraternity alpha to eta Current Opinion in Cell Biology 13 1 49 54 doi 10 1016 S0955 0674 00 00173 3 PMID 11163133 Miller FD Naus CC Durand M Bloom FE Milner RJ December 1987 Isotypes of alpha tubulin are differentially regulated during neuronal maturation The Journal of Cell Biology 105 6 Pt 2 3065 73 doi 10 1083 jcb 105 6 3065 PMC 2114727 PMID 3693406 Cowan NJ Dobner PR Fuchs EV Cleveland DW October 1983 Expression of human alpha tubulin genes interspecies conservation of 3 untranslated regions Molecular and Cellular Biology 3 10 1738 45 doi 10 1128 mcb 3 10 1738 PMC 370035 PMID 6646120 Alexandrova N Niklinski J Bliskovsky V Otterson GA Blake M Kaye FJ Zajac Kaye M September 1995 The N terminal domain of c Myc associates with alpha tubulin and microtubules in vivo and in vitro Molecular and Cellular Biology 15 9 5188 95 doi 10 1128 MCB 15 9 5188 PMC 230766 PMID 7651436 Sapir T Elbaum M Reiner O December 1997 Reduction of microtubule catastrophe events by LIS1 platelet activating factor acetylhydrolase subunit The EMBO Journal 16 23 6977 84 doi 10 1093 emboj 16 23 6977 PMC 1170301 PMID 9384577 Kinnunen T Kaksonen M Saarinen J Kalkkinen N Peng HB Rauvala H April 1998 Cortactin Src kinase signaling pathway is involved in N syndecan dependent neurite outgrowth The Journal of Biological Chemistry 273 17 10702 8 doi 10 1074 jbc 273 17 10702 PMID 9553134 Faruki S Geahlen RL Asai DJ July 2000 Syk dependent phosphorylation of microtubules in activated B lymphocytes Journal of Cell Science 113 14 2557 65 doi 10 1242 jcs 113 14 2557 PMID 10862713 Watts NR Sackett DL Ward RD Miller MW Wingfield PT Stahl SS Steven AC July 2000 HIV 1 rev depolymerizes microtubules to form stable bilayered rings The Journal of Cell Biology 150 2 349 60 doi 10 1083 jcb 150 2 349 PMC 2180222 PMID 10908577 Germani A Bruzzoni Giovanelli H Fellous A Gisselbrecht S Varin Blank N Calvo F December 2000 SIAH 1 interacts with alpha tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis Oncogene 19 52 5997 6006 doi 10 1038 sj onc 1204002 PMID 11146551 Payton JE Perrin RJ Clayton DF George JM November 2001 Protein protein interactions of alpha synuclein in brain homogenates and transfected cells Brain Research Molecular Brain Research 95 1 2 138 45 doi 10 1016 S0169 328X 01 00257 1 PMID 11687285 Bifulco M Laezza C Stingo S Wolff J February 2002 2 3 Cyclic nucleotide 3 phosphodiesterase a membrane bound microtubule associated protein and membrane anchor for tubulin Proceedings of the National Academy of Sciences of the United States of America 99 4 1807 12 Bibcode 2002PNAS 99 1807B doi 10 1073 pnas 042678799 PMC 122275 PMID 11842207 Saugstad JA Yang S Pohl J Hall RA Conn PJ March 2002 Interaction between metabotropic glutamate receptor 7 and alpha tubulin Journal of Neurochemistry 80 6 980 8 doi 10 1046 j 0022 3042 2002 00778 x PMC 2925652 PMID 11953448 Ivings L Pennington SR Jenkins R Weiss JL Burgoyne RD May 2002 Identification of Ca2 dependent binding partners for the neuronal calcium sensor protein neurocalcin delta interaction with actin clathrin and tubulin The Biochemical Journal 363 Pt 3 599 608 doi 10 1042 0264 6021 3630599 PMC 1222513 PMID 11964161 External links EditOverview of all the structural information available in the PDB for UniProt Q71U36 Human Tubulin alpha 1A chain at the PDBe KB Overview of all the structural information available in the PDB for UniProt P68369 Mouse Tubulin alpha 1A chain at the PDBe KB Retrieved from https en wikipedia org w index php title Tubulin alpha 1A chain amp oldid 1081571142, wikipedia, wiki, book, books, library,
