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ITGB1BP1  -  integrin beta 1 binding protein 1

Homo sapiens

Synonyms: ICAP-1, ICAP-1A, ICAP-1B, ICAP-1alpha, ICAP1, ...
 
 
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High impact information on ITGB1BP1

  • Two isoforms of ICAP-1, a 200-amino acid protein (ICAP-1alpha) and a shorter 150-amino acid protein (ICAP-1beta), derived from alternatively spliced mRNA, are expressed in most cells [1].
  • We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain- associated protein-1), which binds to the 1 integrin cytoplasmic domain [1].
  • Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding [1].
  • The regulation of ICAP-1alpha phosphorylation by the cell-matrix interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion [1].
  • CCM2 and ICAP1 bound to CCM1 via their respective PTB domains differentially influence the subcellular localization of CCM1 [2].
 

Biological context of ITGB1BP1

 

Anatomical context of ITGB1BP1

 

Associations of ITGB1BP1 with chemical compounds

  • The alpha isoform of ICAP-1 is a 200 amino acid serine/threonine-rich phosphoprotein which binds the cytoplasmic tail of beta1 integrins [4].
  • ICAP-1 is a ubiquitously expressed protein of 27 and 31 kDa, with the smaller form being preferentially solubilized by Triton X-100 [6].
  • The integrin cytoplasmic domain-associated protein-1 (ICAP-1) binds via its C-terminal PTB (phosphotyrosine-binding) domain to the cytoplasmic tails of beta1 but not other integrins [8].
  • The structure change during the growth processes was observed by transmission electron microscopy (TEM) and the variation in concentrations of gold species in the aqueous solution was monitored by UV-vis spectra and Inductively Coupled Argon Plasma Emission Spectrophotometer (ICAP) [9].
 

Other interactions of ITGB1BP1

 

Analytical, diagnostic and therapeutic context of ITGB1BP1

  • Interestingly, ICAP-1 also is observed in the nucleus, by immunocytochemical staining, and after biochemical cell fractionation, suggesting that it has additional roles that have yet to be determined [5].
  • Using the yeast two-hybrid assay, we found that ICAP-1 binds the ROCK-I kinase, an effector of the RhoA GTPase [8].
  • METHOD: The agreement between the ICAP and the PCR costs measurement was evaluated using the concordance correlation coefficient rho(c) [13].
  • Although the sample size was small, the results are encouraging and suggest further development of the intervention, Interaction Coaching for Adolescent Parents and their Infants (ICAP) [14].

References

  1. ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin. Chang, D.D., Wong, C., Smith, H., Liu, J. J. Cell Biol. (1997) [Pubmed]
  2. CCM1 and CCM2 protein interactions in cell signaling: implications for cerebral cavernous malformations pathogenesis. Zawistowski, J.S., Stalheim, L., Uhlik, M.T., Abell, A.N., Ancrile, B.B., Johnson, G.L., Marchuk, D.A. Hum. Mol. Genet. (2005) [Pubmed]
  3. Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation. Zhang, J., Clatterbuck, R.E., Rigamonti, D., Chang, D.D., Dietz, H.C. Hum. Mol. Genet. (2001) [Pubmed]
  4. KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis. Zawistowski, J.S., Serebriiskii, I.G., Lee, M.F., Golemis, E.A., Marchuk, D.A. Hum. Mol. Genet. (2002) [Pubmed]
  5. Nuclear translocation of integrin cytoplasmic domain-associated protein 1 stimulates cellular proliferation. Fournier, H.N., Dupé-Manet, S., Bouvard, D., Luton, F., Degani, S., Block, M.R., Retta, S.F., Albiges-Rizo, C. Mol. Biol. Cell (2005) [Pubmed]
  6. Interaction of the integrin beta1 cytoplasmic domain with ICAP-1 protein. Zhang, X.A., Hemler, M.E. J. Biol. Chem. (1999) [Pubmed]
  7. Disruption of focal adhesions by integrin cytoplasmic domain-associated protein-1 alpha. Bouvard, D., Vignoud, L., Dupé-Manet, S., Abed, N., Fournier, H.N., Vincent-Monegat, C., Retta, S.F., Fassler, R., Block, M.R. J. Biol. Chem. (2003) [Pubmed]
  8. Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane. Stroeken, P.J., Alvarez, B., Van Rheenen, J., Wijnands, Y.M., Geerts, D., Jalink, K., Roos, E. J. Cell. Physiol. (2006) [Pubmed]
  9. Formation process of two-dimensional networked gold nanowires by citrate reduction of AuCl4- and the shape stabilization. Pei, L., Mori, K., Adachi, M. Langmuir : the ACS journal of surfaces and colloids. (2004) [Pubmed]
  10. Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement. Fournier, H.N., Dupé-Manet, S., Bouvard, D., Lacombe, M.L., Marie, C., Block, M.R., Albiges-Rizo, C. J. Biol. Chem. (2002) [Pubmed]
  11. Sorting nexin 17, a non-self-assembling and a PtdIns(3)P high class affinity protein, interacts with the cerebral cavernous malformation related protein KRIT1. Czubayko, M., Knauth, P., Schlüter, T., Florian, V., Bohnensack, R. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  12. Differential modulation of integrin expression in chondrocytes during expansion for tissue engineering. Goessler, U.R., Bugert, P., Bieback, K., Huber, K., Fleischer, L.I., Hormann, K., Riedel, F. In Vivo (2005) [Pubmed]
  13. Collecting psychiatric resources utilisation data to calculate costs of care: a comparison between a service receipt interview and a case register. Mirandola, M., Bisoffi, G., Bonizzato, P., Amaddeo, F. Social psychiatry and psychiatric epidemiology. (1999) [Pubmed]
  14. Strategy for promoting greater responsiveness in adolescent parent/infant relationships: report of a pilot study. Censullo, M. Journal of pediatric nursing. (1994) [Pubmed]
 
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