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Integrin beta 1 binding protein 1

ICAP-1, integrin cytoplasmic domain-associated protein-1, ICAP1alpha
The cytoplasmic domains of integrins are essential for cell adhesion. The protein encoded by this gene binds to the beta1 integrin cytoplasmic domain. The interaction between this protein and beta1 integrin is highly specific. Two isoforms of this protein are derived from alternatively spliced transcripts. The shorter form of this protein does not interact with the beta1 integrin cytoplasmic domain. The longer form is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-matrix interaction, suggesting an important role of this protein during integrin-dependent cell adhesion. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fibronectin, CAN, PTB, vitronectin, Rap1
Papers on ICAP-1
In vivo adhesion of malignant B cells to bone marrow microvasculature is regulated by α4β1 cytoplasmic-binding proteins.
Teixidó et al., Madrid, Spain. In Leukemia, Jan 2016
Talin, kindlin-3 and ICAP-1 are β1-integrin-binding partners that regulate β1-mediated cell adhesion.
CCM1-ICAP-1 complex controls β1 integrin-dependent endothelial contractility and fibronectin remodeling.
Albiges-Rizo et al., Grenoble, France. In J Cell Biol, 2013
Association of the CCM1/2 complex with ICAP-1, an inhibitor of β1 integrin, prompted us to investigate whether the CCM complex interferes with integrin signaling.
Calcium and calmodulin-dependent serine/threonine protein kinase type II (CaMKII)-mediated intramolecular opening of integrin cytoplasmic domain-associated protein-1 (ICAP-1α) negatively regulates β1 integrins.
Bouvard et al., Grenoble, France. In J Biol Chem, 2013
Focal adhesion turnover during cell migration is an integrated cyclic process requiring tight regulation of integrin function.
Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide.
Boggon et al., New Haven, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013
Integrin cytoplasmic domain-associated protein-1 (ICAP1) is a suppressor of integrin activation and directly binds to the cytoplasmic tail of β1 integrins; its binding suppresses integrin activation by competition with talin.
Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation.
Boggon et al., New Haven, United States. In Mol Cell, 2013
We show that KRIT1 functions as a switch for β1 integrin activation by antagonizing ICAP1 (Integrin Cytoplasmic Associated Protein-1)-mediated modulation of "inside-out" activation.
Concepts and hypothesis: integrin cytoplasmic domain-associated protein-1 (ICAP-1) as a potential player in cerebral cavernous malformation.
Wang et al., Chongqing, China. In J Neurol, 2013
Recent studies have shown that integrin cytoplasmic domain-associated protein-1 (ICAP-1, also known as integrin β1 binding protein1, ITGB1BP), a cytoplasmic protein interacting with both β1 integrin subunit and CCM1 protein (also known as Krit1), is implicated in vascular development.
Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition.
Bouvard et al., Grenoble, France. In J Cell Biol, 2011
The ICAP-1 works in concert with kindlin-2 to control the dynamics of beta1 integrin-containing fibrillar adhesions and, thereby, regulates fibronectin deposition and osteoblast mineralization.
Integrin cytoplasmic domain-associated protein-1 attenuates sprouting angiogenesis.
Fischer et al., Mannheim, Germany. In Circ Res, 2010
Identify ICAP1 as a novel regulator to prevent excessive sprouting angiogenesis.
Role of nm23 in the regulation of cell shape and migration via Rho family GTPase signals.
Ono et al., Kōbe, Japan. In Mol Cell Biochem, 2009
Furthermore, we found that Lbc, nm23-H2 and ICAP1-alpha could form tertial complex in cells, and this complex formation was thought to be critical for cell migration stimulated by integrin.
Krit1 modulates beta 1-integrin-mediated endothelial cell proliferation.
Clatterbuck et al., Jackson, United States. In Neurosurgery, 2008
integrin cytoplasmic domain-associated protein-1 alpha (icap1alpha) act concordantly to play a critical role in beta1-integrin-mediated cell proliferation.
Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes migration of myoblasts and affects focal adhesions.
Roos et al., Amsterdam, Netherlands. In J Cell Physiol, 2008
ICAP-1 regulates beta1 integrin-dependent cell migration by affecting the pattern of focal adhesion formation.
Cell adaptive response to extracellular matrix density is controlled by ICAP-1-dependent beta1-integrin affinity.
Albiges-Rizo et al., France. In J Cell Biol, 2008
Live cell imaging, which was performed in both Icap-1-deficient mouse embryonic fibroblasts and cells expressing active beta(1) integrin, shows that the integrin high affinity state favored by talin is antagonistically controlled by ICAP-1.
Krit 1 interactions with microtubules and membranes are regulated by Rap1 and integrin cytoplasmic domain associated protein-1.
Faurobert et al., France. In Febs J, 2007
We show that a ternary complex can form in vitro between Krit1, Rap1 and ICAP-1 and that Rap1 binds the Krit1 FERM domain in both closed and opened conformations.
Proteomic identification of the cerebral cavernous malformation signaling complex.
Wu et al., Chapel Hill, United States. In J Proteome Res, 2007
Previously identified proteins that associate with OSM including KRIT1, MEKK3, Rac, and the KRIT1-binding protein ICAP-1 were found in the immunoprecipitates.
Unraveling ICAP-1 function: toward a new direction?
Albiges-Rizo et al., France. In Eur J Cell Biol, 2006
Integrin cytoplasmic domain-associated protein-1 (ICAP-1) is a small cytoplasmic protein that specifically interacts with the beta1 integrin subunit.
New insights into Nm23 control of cell adhesion and migration.
Block et al., Grenoble, France. In J Bioenerg Biomembr, 2003
Finally, the recent discovery of the interaction between Nm23-H2 and the negative regulator of beta1 integrin-mediated cell adhesion, ICAP-1, which targets the kinase to lamellipodia and cell protrusions, suggests that the Nm23-H2/ICAP-1 complex plays a role in integrin signaling, and exerts a fine-tuning between migration and spreading.
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