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Gene Review

ITGB3BP  -  integrin beta 3 binding protein (beta3...

Homo sapiens

Synonyms: Beta-3-endonexin, CENP-R, CENPR, Centromere protein R, HSU37139, ...
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Disease relevance of ITGB3BP

  • In addition, NRIF3 deregulation enhanced the responsiveness of breast cancer cells to estrogen-induced stimulation of growth and anchorage independence [1].
  • Here, we show that the long form of beta3-endonexin (EN-L) can be detected in platelet lysates several hours after thrombus formation, after long-term storage of platelets and after glucose deprivation [2].

High impact information on ITGB3BP

  • The cytoplasmic domains of integrins are required for the transduction of this bidirectional information, and have recently been shown to participate in direct interactions with some novel cytoplasmic proteins, such as an ankyrin repeat containing serine/threonine protein kinase (integrin-linked kinase) and beta3 endonexin [3].
  • Thus, the discovery of TAP20, which interacts with integrin beta5 and modulates cell adhesion, migration, and tube formation, further defines a possible pathway to angiogenesis dependent on PKCtheta [4].
  • Enhancement of endothelial cell migration and in vitro tube formation by TAP20, a novel beta 5 integrin-modulating, PKC theta-dependent protein [4].
  • Overexpression of TAP20 also decreased focal adhesion formation in alphavbeta3-deficient cells [4].
  • Affinity modulation of alphaIIbbeta3 by GFP/beta3-endonexin was inhibited by coexpression of either a monomeric beta3 cytoplasmic tail chimera or an activated form of H-Ras [5].

Biological context of ITGB3BP

  • By using Gal4 fusion constructs, we identified an autonomous transactivation domain (AD1) at the C terminus of NRIF3 [6].
  • The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells [7].
  • Domain and mutagenesis analyses indicated that a novel C-terminal domain in NRIF3 plays an essential role in its specific interaction with liganded TR and RXR while the N-terminal LXXLL motif plays a minor role in allowing optimum interaction [8].
  • The NRIF3 gene encodes at least two additional isoforms due to alternative splicing [6].
  • Interestingly, a single amino acid residue change of a potential phosphorylation site in RepD1 (Ser(28) to Ala) abolishes its transrepression function, suggesting that the coregulatory property of NRIF3 (or its isoforms) might be subjected to regulation by cellular signaling [6].

Anatomical context of ITGB3BP


Associations of ITGB3BP with chemical compounds


Physical interactions of ITGB3BP

  • NRIF3 interacted with MTA1 both in vitro and in vivo [1].
  • This process may be triggered by a regulatory molecule(s) that binds to the integrin cytoplasmic tails, causing a structural change in the receptor. beta3-Endonexin is a novel 111-amino acid protein that binds selectively to the beta3 tail [5].

Regulatory relationships of ITGB3BP

  • MTA1 repressed NRIF3-mediated stimulation of ERE-driven transcription and interfered with NRIF3's association with the ER target gene chromatin [1].

Other interactions of ITGB3BP


Analytical, diagnostic and therapeutic context of ITGB3BP


  1. Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator. Talukder, A.H., Gururaj, A., Mishra, S.K., Vadlamudi, R.K., Kumar, R. Mol. Cell. Biol. (2004) [Pubmed]
  2. Proteolysis leads to the appearance of the long form of beta3-endonexin in human platelets. Sadoul, K., Vignoud, L., Mossuz, P., Block, M.R. Exp. Cell Res. (2005) [Pubmed]
  3. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Dedhar, S., Hannigan, G.E. Curr. Opin. Cell Biol. (1996) [Pubmed]
  4. Enhancement of endothelial cell migration and in vitro tube formation by TAP20, a novel beta 5 integrin-modulating, PKC theta-dependent protein. Tang, S., Gao, Y., Ware, J.A. J. Cell Biol. (1999) [Pubmed]
  5. Affinity modulation of platelet integrin alphaIIbbeta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tail. Kashiwagi, H., Schwartz, M.A., Eigenthaler, M., Davis, K.A., Ginsberg, M.H., Shattil, S.J. J. Cell Biol. (1997) [Pubmed]
  6. Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation. Li, D., Wang, F., Samuels, H.H. Mol. Cell. Biol. (2001) [Pubmed]
  7. The NRIF3 family of transcriptional coregulators induces rapid and profound apoptosis in breast cancer cells. Li, D., Das, S., Yamada, T., Samuels, H.H. Mol. Cell. Biol. (2004) [Pubmed]
  8. NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors. Li, D., Desai-Yajnik, V., Lo, E., Schapira, M., Abagyan, R., Samuels, H.H. Mol. Cell. Biol. (1999) [Pubmed]
  9. Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit. Shattil, S.J., O'Toole, T., Eigenthaler, M., Thon, V., Williams, M., Babior, B.M., Ginsberg, M.H. J. Cell Biol. (1995) [Pubmed]
  10. beta3-endonexin as a novel inhibitor of cyclin A-associated kinase. Ohtoshi, A., Maeda, T., Higashi, H., Ashizawa, S., Yamada, M., Hatakeyama, M. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
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