The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

BAIAP2  -  BAI1-associated protein 2

Homo sapiens

Synonyms: BAI-associated protein 2, BAP2, Brain-specific angiogenesis inhibitor 1-associated protein 2, FLAF3, Fas ligand-associated factor 3, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of BAIAP2

  • Five proteins including IRSp53 and missing in metastasis (MIM) protein share this unique domain and are highly conserved in vertebrates [1].
  • In addition, IRSp53/Eps8 complex formation as determined by fluorescent resonance energy transfer analysis, occurs at the leading edge of motile cells, and the motility and invasiveness of HT1080 fibrosarcoma cells are suppressed by inhibiting complex formation [2].
  • We found that although Salmonella infection strongly promotes the formation of an IRSp53/WAVE2 complex, IRSp53 is not necessary for bacterial internalization [3].
  • The biological roles of BAP2 propeptide and mature peptide have been investigated by heterologous expression of the proprotein in Escherichia coli, and by tests of its fungistatic activity and that of the fully processed form in vitro [4].

High impact information on BAIAP2


Biological context of BAIAP2

  • Using its intracellular carboxyl terminus as "bait" in a yeast two-hybrid system, we isolated a cDNA clone named BAIAP2 whose nucleotide sequence would encode a 521-amino acid protein showing significant homology to a 58/53-kDa substrate of insulin-receptor kinase in the hamster [8].
  • In vitro binding assays confirmed that a proline-rich cytoplasmic fragment of BAI1 interacted with the Src homology 3 (SH3) domain of BAIAP2 [8].
  • IRS-58 is a brain-enriched protein comprising at least four protein-protein interaction sites: a Cdc42Hs binding site, an Src homology (SH)3-binding site, an SH3 domain, and a tryptophan, tyrptophan (WW)-binding domain [9].
  • Here, we search for other binding partners for the IRSp53 SH3 domain and identify Eps8 as the major binding protein in fibroblasts and various cancer cell lines [2].
  • Our analysis of IRSp58/53 mRNA suggests that within rat brain there is one coding region for IRSp58 and IRSp53; we find no evidence of alternative splicing [10].

Anatomical context of BAIAP2


Associations of BAIAP2 with chemical compounds

  • IRSp53 and BAIAP2 have independently been isolated as a 58/53-kDa protein tyrosine phosphorylated in response to insulin and a BAI1-binding protein, respectively [12].
  • A proline-rich region near the polyglutamine tract of the DRPLA protein and the SH3 domain of IRSp53 were involved in the binding [13].

Physical interactions of BAIAP2


Regulatory relationships of BAIAP2


Other interactions of BAIAP2


Analytical, diagnostic and therapeutic context of BAIAP2


  1. A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. Yamagishi, A., Masuda, M., Ohki, T., Onishi, H., Mochizuki, N. J. Biol. Chem. (2004) [Pubmed]
  2. IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness. Funato, Y., Terabayashi, T., Suenaga, N., Seiki, M., Takenawa, T., Miki, H. Cancer Res. (2004) [Pubmed]
  3. WAVE2 signaling mediates invasion of polarized epithelial cells by Salmonella typhimurium. Shi, J., Scita, G., Casanova, J.E. J. Biol. Chem. (2005) [Pubmed]
  4. Maize endosperm secretes a novel antifungal protein into adjacent maternal tissue. Serna, A., Maitz, M., O'Connell, T., Santandrea, G., Thevissen, K., Tienens, K., Hueros, G., Faleri, C., Cai, G., Lottspeich, F., Thompson, R.D. Plant J. (2001) [Pubmed]
  5. Missing-in-metastasis and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain-like mechanism. Mattila, P.K., Pykäläinen, A., Saarikangas, J., Paavilainen, V.O., Vihinen, H., Jokitalo, E., Lappalainen, P. J. Cell Biol. (2007) [Pubmed]
  6. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. Suetsugu, S., Kurisu, S., Oikawa, T., Yamazaki, D., Oda, A., Takenawa, T. J. Cell Biol. (2006) [Pubmed]
  7. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. Millard, T.H., Bompard, G., Heung, M.Y., Dafforn, T.R., Scott, D.J., Machesky, L.M., Fütterer, K. EMBO J. (2005) [Pubmed]
  8. Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1. Oda, K., Shiratsuchi, T., Nishimori, H., Inazawa, J., Yoshikawa, H., Taketani, Y., Nakamura, Y., Tokino, T. Cytogenet. Cell Genet. (1999) [Pubmed]
  9. Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin. Govind, S., Kozma, R., Monfries, C., Lim, L., Ahmed, S. J. Cell Biol. (2001) [Pubmed]
  10. The insulin receptor tyrosine kinase substrate p58/53 and the insulin receptor are components of CNS synapses. Abbott, M.A., Wells, D.G., Fallon, J.R. J. Neurosci. (1999) [Pubmed]
  11. Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex. Krugmann, S., Jordens, I., Gevaert, K., Driessens, M., Vandekerckhove, J., Hall, A. Curr. Biol. (2001) [Pubmed]
  12. Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2. Fujiwara, T., Mammoto, A., Kim, Y., Takai, Y. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  13. Dentatorubral-pallidoluysian atrophy protein interacts through a proline-rich region near polyglutamine with the SH3 domain of an insulin receptor tyrosine kinase substrate. Okamura-Oho, Y., Miyashita, T., Ohmi, K., Yamada, M. Hum. Mol. Genet. (1999) [Pubmed]
  14. The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein cdc42. Soltau, M., Richter, D., Kreienkamp, H.J. Mol. Cell. Neurosci. (2002) [Pubmed]
  15. MALS is a binding partner of IRSp53 at cell-cell contacts. Hori, K., Konno, D., Maruoka, H., Sobue, K. FEBS Lett. (2003) [Pubmed]
  16. Insulin receptor substrate of 53 kDa links postsynaptic shank to PSD-95. Soltau, M., Berhörster, K., Kindler, S., Buck, F., Richter, D., Kreienkamp, H.J. J. Neurochem. (2004) [Pubmed]
WikiGenes - Universities