BAIAP2

From Wikipedia, the free encyclopedia

BAI1-associated protein 2

PDB rendering based on 1wdz.

Available structures: 1wdz, 1y2o

Identifiers

Symbol(s)

BAIAP2; BAP2; IRSP53

External IDs

OMIM: 605475 MGI: 2137336 HomoloGene: 9697

Gene ontology
Molecular Function:	• protein C-terminus binding • cytoskeletal adaptor activity
Cellular Component:	• cytoplasm • plasma membrane
Biological Process:	• axonogenesis • insulin receptor signaling pathway

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006340 (mRNA)
NP_006331 (protein)

NM_001037754 (mRNA)
NP_001032843 (protein)

Location

Chr 17: 76.62 - 76.71 Mb

Chr 11: 119.76 - 119.82 Mb

Pubmed search

[1]

[2]

BAI1-associated protein 2, also known as BAIAP2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: BAIAP2 BAI1-associated protein 2.

[edit] 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): 171-4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Okamura-Oho Y, Miyashita T, Ohmi K, Yamada M (1999). "Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate.". Hum. Mol. Genet. 8 (6): 947-57. PMID 10332026.
Oda K, Shiratsuchi T, Nishimori H, et al. (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.". Cytogenet. Cell Genet. 84 (1-2): 75-82. PMID 10343108.
Abbott MA, Wells DG, Fallon JR (1999). "The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses.". J. Neurosci. 19 (17): 7300-8. 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.". Biochem. Biophys. Res. Commun. 271 (3): 626-9. doi:10.1006/bbrc.2000.2671. PMID 10814512.
Miki H, Yamaguchi H, Suetsugu S, Takenawa T (2001). "IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling.". Nature 408 (6813): 732-5. doi:10.1038/35047107. PMID 11130076.
Govind S, Kozma R, Monfries C, et al. (2001). "Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin.". J. Cell Biol. 152 (3): 579-94. PMID 11157984.
Krugmann S, Jordens I, Gevaert K, et al. (2002). "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex.". Curr. Biol. 11 (21): 1645-55. PMID 11696321.
Miki H, Takenawa T (2002). "WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac.". Biochem. Biophys. Res. Commun. 293 (1): 93-9. doi:10.1016/S0006-291X(02)00218-8. PMID 12054568.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Soltau M, Richter D, Kreienkamp HJ (2003). "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42.". Mol. Cell. Neurosci. 21 (4): 575-83. PMID 12504591.
Sekerková G, Loomis PA, Changyaleket B, et al. (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.". J. Neurosci. 23 (4): 1310-9. PMID 12598619.
Miyahara A, Okamura-Oho Y, Miyashita T, et al. (2003). "Genomic structure and alternative splicing of the insulin receptor tyrosine kinase substrate of 53-kDa protein.". J. Hum. Genet. 48 (8): 410-4. 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 Lett. 554 (1-2): 30-4. PMID 14596909.
Lehner B, Semple JI, Brown SE, et al. (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): 153-67. PMID 14667819.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Yamagishi A, Masuda M, Ohki T, et al. (2004). "A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein.". J. Biol. Chem. 279 (15): 14929-36. doi:10.1074/jbc.M309408200. PMID 14752106.
Funato Y, Terabayashi T, Suenaga N, et al. (2004). "IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness.". Cancer Res. 64 (15): 5237-44. doi:10.1158/0008-5472.CAN-04-0327. PMID 15289329.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436-50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.