BAIAP2
Brain-specific angiogenesis inhibitor 1-associated protein 2 is a protein that in humans is encoded by the BAIAP2 gene.[5][6]
Function
The protein encoded by this gene has been identified as a brain-specific angiogenesis inhibitor (BAI1)-binding protein. This interaction at the cytoplasmic membrane is crucial to the function of this protein, which may be involved in neuronal growth-cone guidance. This protein functions as an insulin receptor tyrosine kinase substrate and suggests a role for insulin in the central nervous system. This protein has also been identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is associated with an autosomal dominant neurodegenerative disease. It also associates with a downstream effector of Rho small G proteins, which is associated with the formation of stress fibers and cytokinesis. Alternative splicing of the 3'-end of this gene results in three products of undetermined function.[6] The I-BAR/IMD domain of BAIAP2/IRSp53 binds to and deform the plasma membrane for cellular protrusions.[7]
Interactions
BAIAP2 has been shown to interact with:
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000175866 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025372 – 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.
- ^ Oda K, Shiratsuchi T, Nishimori H, Inazawa J, Yoshikawa H, Taketani Y, et al. (June 1999). "Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1". Cytogenetics and Cell Genetics. 84 (1–2): 75–82. doi:10.1159/000015219. PMID 10343108. S2CID 27688560.
- ^ a b "Entrez Gene: BAIAP2 BAI1-associated protein 2".
- ^ Suetsugu S, Murayama K, Sakamoto A, Hanawa-Suetsugu K, Seto A, Oikawa T, et al. (November 2006). "The RAC binding domain/IRSp53-MIM homology domain of IRSp53 induces RAC-dependent membrane deformation". The Journal of Biological Chemistry. 281 (46) (published 2006): 35347–35358. doi:10.1074/jbc.M606814200. PMID 17003044.
- ^ Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M (June 1999). "Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate". Human Molecular Genetics. 8 (6): 947–957. doi:10.1093/hmg/8.6.947. PMID 10332026.
- ^ a b c d Miki H, Yamaguchi H, Suetsugu S, Takenawa T (December 2000). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling". Nature. 408 (6813): 732–735. Bibcode:2000Natur.408..732M. doi:10.1038/35047107. PMID 11130076. S2CID 4426046.
- ^ a b Soltau M, Richter D, Kreienkamp HJ (December 2002). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42". Molecular and Cellular Neurosciences. 21 (4): 575–583. doi:10.1006/mcne.2002.1201. PMID 12504591. S2CID 572407.
- ^ Krugmann S, Jordens I, Gevaert K, Driessens M, Vandekerckhove J, Hall A (October 2001). "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex". Current Biology. 11 (21): 1645–1655. doi:10.1016/S0960-9822(01)00506-1. PMID 11696321. S2CID 11290377.
- ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
- ^ Funato Y, Terabayashi T, Suenaga N, Seiki M, Takenawa T, Miki H (August 2004). "IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness". Cancer Research. 64 (15): 5237–5244. doi:10.1158/0008-5472.CAN-04-0327. PMID 15289329. S2CID 9844872.
External links
- Human BAIAP2 genome location and BAIAP2 gene details page in the UCSC Genome Browser.
Further reading
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Abbott MA, Wells DG, Fallon JR (1999). "The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses". The Journal of Neuroscience. 19 (17): 7300–7308. doi:10.1523/JNEUROSCI.19-17-07300.1999. PMC 6782521. PMID 10460236.
- Fujiwara T, Mammoto A, Kim Y, Takai Y (2000). "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2". Biochemical and Biophysical Research Communications. 271 (3): 626–629. doi:10.1006/bbrc.2000.2671. PMID 10814512.
- Govind S, Kozma R, Monfries C, Lim L, Ahmed S (February 2001). "Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin". The Journal of Cell Biology. 152 (3): 579–594. doi:10.1083/jcb.152.3.579. PMC 2195994. PMID 11157984.
- Miki H, Takenawa T (2002). "WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac". Biochemical and Biophysical Research Communications. 293 (1): 93–99. doi:10.1016/S0006-291X(02)00218-8. PMID 12054568.
- Sekerková G, Loomis PA, Changyaleket B, Zheng L, Eytan R, Chen B, et al. (February 2003). "Novel espin actin-bundling proteins are localized to Purkinje cell dendritic spines and bind the Src homology 3 adapter protein insulin receptor substrate p53". The Journal of Neuroscience. 23 (4): 1310–1319. doi:10.1523/JNEUROSCI.23-04-01310.2003. PMC 2854510. PMID 12598619.
- Miyahara A, Okamura-Oho Y, Miyashita T, Hoshika A, Yamada M (2003). "Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein". Journal of Human Genetics. 48 (8): 410–414. doi:10.1007/s10038-003-0047-x. PMID 12884081.
- Hori K, Konno D, Maruoka H, Sobue K (2003). "MALS is a binding partner of IRSp53 at cell-cell contacts". FEBS Letters. 554 (1–2): 30–34. doi:10.1016/S0014-5793(03)01074-3. PMID 14596909. S2CID 30329043.
- Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics. 83 (1): 153–167. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
- Yamagishi A, Masuda M, Ohki T, Onishi H, Mochizuki N (April 2004). "A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein". The Journal of Biological Chemistry. 279 (15): 14929–14936. doi:10.1074/jbc.M309408200. PMID 14752106.
- Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, et al. (August 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–1450. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
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