The Rap1-RIAM-talin axis of integrin activation and blood cell function.
TLDR
Recent progress in understanding the mechanisms of integrin activation with a focus on the functions of blood cells is reviewed, including how talin binding to the integrin β cytoplasmic domain, in conjunction with the plasma membrane, induces long-range allosteric rearrangements that lead to integrinactivation.About:
This article is published in Blood.The article was published on 2016-07-28 and is currently open access. It has received 108 citations till now. The article focuses on the topics: Integrin, beta 6 & Integrin alpha M.read more
Citations
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Journal ArticleDOI
Integrin activation by talin, kindlin and mechanical forces
TL;DR: The current understanding of how talin, kindlin and mechanical forces regulate integrin affinity and avidity is discussed, and how integrin inactivators function in this framework.
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Phagocytosis: A Fundamental Process in Immunity
TL;DR: A general view of the current knowledge on phagocytosis is presented and novel molecular findings, particularly on phagosome formation and maturation are emphasized, and aspects that remain incompletely understood are discussed.
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Phagocytosis: Our Current Understanding of a Universal Biological Process.
TL;DR: A general view of the current understanding on cells, phagocytic receptors and phases involved inphagocytosis is presented.
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Talin – the master of integrin adhesions
TL;DR: The mechano-sensitive structure of talin provides a paradigm for how proteins transduce mechanical signals to chemical signals, while functioning at many levels in the extracellular matrix–cytoskeleton linkage.
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Integrin αIIbβ3 outside-in signaling
TL;DR: This review provides a concise but comprehensive overview of αIIbβ3 outside-in signaling, focusing on the key players involved, and how they cooperate to orchestrate this critical aspect of platelet biology.
References
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Journal ArticleDOI
Integrins: Bidirectional, Allosteric Signaling Machines
TL;DR: Current structural and cell biological data suggest models for how integrins transmit signals between their extracellular ligand binding adhesion sites and their cytoplasmic domains, which link to the cytoskeleton and to signal transduction pathways.
Journal ArticleDOI
Lipid Rafts As a Membrane-Organizing Principle
Daniel Lingwood,Kai Simons +1 more
TL;DR: The evidence for how this principle combines the potential for sphingolipid-cholesterol self-assembly with protein specificity to selectively focus membrane bioactivity is reviewed.
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Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
J. de Rooij,Fried J. T. Zwartkruis,M. H. G. Verheijen,Robbert H. Cool,Sebastian M.B. Nijman,Alfred Wittinghofer,Johannes L. Bos +6 more
TL;DR: The cloned gene encoding a guanine-nucleotide-exchange factor (GEF) for Rap1 is named Epac, which contains a cAMP-binding site and a domain that is homologous to domains of known GEFs for Ras and Rap1 that is regulated directly by cAMP.
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Platelet Activation and Atherothrombosis
Giovanni Davì,Carlo Patrono +1 more
TL;DR: This review of the role of platelets in at Herothrombosis illuminates the surprisingly numerous activities of these tiny, anucleate cells and stresses their participation in the inflammatory component of atherothromBosis.
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Structural Basis of Integrin Regulation and Signaling
TL;DR: This review focuses on integrin structure as it relates to affinity modulation, ligand binding, outside-in signaling, and cell surface distribution dynamics.