Integrin Cytoplasmic Tail Interactions

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Integrin Cytoplasmic Tail Interactions

Integrins are heterodimeric cell surface adhesion receptors essential for multicellular life. They connect cells to the extracellular environment and transduce chemical and mechanical signals to and from the cell. Intracellular proteins that bind the integrin cytoplasmic tail regulate integrin engagement of extracellular ligands as well as integrin localization and trafficking. Cytoplasmic inte...

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Integrin Cytoplasmic Tail

Platelet agonists increase the affinity state of integrin a IIb b 3 , a prerequisite for fibrinogen binding and platelet aggregation. This process may be triggered by a regulatory molecule(s) that binds to the integrin cytoplasmic tails, causing a structural change in the receptor. b 3 -Endonexin is a novel 111–amino acid protein that binds selectively to the b 3 tail. Since b 3 -endonexin is p...

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Vimentin filaments regulate integrin-ligand interactions by binding to the cytoplasmic tail of integrin β3.

Vimentin, an intermediate filament protein induced during epithelial-to-mesenchymal transition, is known to regulate cell migration and invasion. However, it is still unclear how vimentin controls such behaviors. In this study, we aimed to find a new integrin regulator by investigating the H-Ras-mediated integrin suppression mechanism. Through a proteomic screen using the integrin β3 cytoplasmi...

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Direct interactions with the integrin β1 cytoplasmic tail activate the Abl2/Arg kinase.

Integrins are heterodimeric α/β extracellular matrix adhesion receptors that couple physically to the actin cytoskeleton and regulate kinase signaling pathways to control cytoskeletal remodeling and adhesion complex formation and disassembly. β1 integrins signal through the Abl2/Arg (Abl-related gene) nonreceptor tyrosine kinase to control fibroblast cell motility, neuronal dendrite morphogenes...

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Suppression of integrin activation by the membrane-distal sequence of the integrin alphaIIb cytoplasmic tail.

Integrin cytoplasmic tails regulate integrin activation including an increase in integrin affinity for ligands. Although there is ample evidence that the membrane-proximal regions of the alpha and beta tails interact with each other to maintain integrins in a low-affinity state, little is known about the role of the membrane-distal region of the alpha tail in regulation of integrin activation. ...

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ژورنال

عنوان ژورنال: Biochemistry

سال: 2014

ISSN: 0006-2960,1520-4995

DOI: 10.1021/bi401596q