Molecular Basis of CIB Binding to the Integrin αIIb Cytoplasmic Domain
نویسندگان
چکیده
منابع مشابه
Integrin cytoplasmic domain-binding proteins.
Integrins are a large family of cell surface receptors that mediate cell adhesion and influence migration, signal transduction, and gene expression. The cytoplasmic domains of integrins play a pivotal role in these integrin-mediated cellular functions. Through interaction with the cytoskeleton, signaling molecules, and other cellular proteins, integrin cytoplasmic domains transduce signals from...
متن کاملCalcium Integrin Binding Protein Associates with Integrins αVβ3 and αIIbβ3 Independent of β3 Activation Motifs.
The Calcium Integrin Binding protein (CIB) has been identified as interacting specifically with the cytoplasmic tail of the integrin αIIb domain to induce receptor activation and integrin αIIbβ3 mediated cell adhesion to extracellular proteins. In K562 cells stably expressing mutated integrin αVβ3, or chimeric αVβ3 carrying αIIb cytoplasmic tail, we report that the interaction of CIB with β3 in...
متن کاملCharacterization of β1 Integrin Cytoplasmic Domain Binding Proteins
Article Chronology:Received 28 March 2006Revised version received6 June 2006Accepted 13 June 2006Available online 29 June 2006The three Kindlins are a novel family of focal adhesion proteins. The Kindlin-1 (URP1) gene ismutated in Kindler syndrome, the first skin blistering disease affecting actin attachment inbasal keratinocytes. Kindlin-2 (Mig-2), the best stud...
متن کاملStructure of the Integrin αIIb Transmembrane Segment
Integrin cell-adhesion receptors transduce signals bidirectionally across the plasma membrane via the single-pass transmembrane segments of each and subunit. While the 3 transmembrane segment consists of a linear 29-residue -helix, the structure of the IIb transmembrane segment reveals a linear 24-residue -helix (Ile-966–Lys-989) followed by a backbone reversal that packs Phe-992–Phe-993 agains...
متن کاملExposure of ligand-binding sites on platelet integrin αIIB/β3 by phosphorylation of the β3 subunit
The exposure of ligand-binding sites for adhesive proteins on platelet integrin α IIB }β $ (glycoprotein IIB}IIIA) by plateletactivating factor (PAF) is transient, whereas sites exposed by αthrombin remain accessible. The same difference is seen in the phosphorylation of the β $ subunit. Inhibition of protein kinases (1 μM staurosporine) and protein kinase C (10 μM bisindolylmaleimide) closes b...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m202983200