Recent advances in the understanding of the molecular mechanisms regulating platelet integrin αIIbβ3 activation
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- 作者：Lanlan Tao (1) (2)
Yue Zhang (1)
Xiaodong Xi (1) (2)
Nelly Kieffer (1) - 刊名：Protein & Cell
- 出版年：2010
- 出版时间：July 2010
- 年：2010
- 卷：1
- 期：7
- 页码：627-637
- 全文大小：365KB
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Yue Zhang (1)
Xiaodong Xi (1) (2)
Nelly Kieffer (1)
1. Sino-French Research Center for Life Sciences and Genomics (CNRS/LIA-124), Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, 200025, China
2. State Key Laboratory of Medical Genomics and Shanghai Institute of Hematology, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, 200025, China
文摘
Integrins are allosteric cell adhesion receptors that cycle from a low to a high affinity ligand binding state, a complex process of receptor activation that is of particular importance in blood cells such as platelets or leukocytes. Here we highlight recent progress in the understanding of the molecular pathways that regulate integrin activation in platelets and leukocytes, with a special focus on the structural changes in platelet integrin αIIbβ3 brought about by key intracellular proteins, namely talin and kindlins, that are of crucial importance in the regulation of integrin function. Evidence that the small GTPase Rap1 and its guanine exchange factor CalDAG-GEF1, together with RIAM, a Rap1GTP adaptor protein, promote the interaction of talin with the integrin β subunit, has greatly contributed to fill the gap in our understanding of the signaling pathway from G-coupled agonist receptors and their phospholipase C-dependant second messengers, to integrin activation. Studies of patients with the rare blood cell disorder LAD-III have contributed to the identification of kindlins as new co-regulators of the talin-dependent integrin activation process in platelets and leukocytes, underlining the relevance for the in-depth investigation of patients with rare genetic blood cell disorders.