Salsmann Alexandre, Schaffner-Reckinger Elisabeth, Kieffer Nelly
Laboratoire de Biologie et Physiologie Intégrée, (CNRS/GDRE-ITI), Université du Luxembourg, 162A, Avenue de la Faïencerie, L-1511 Luxembourg.
Eur J Cell Biol. 2006 Apr;85(3-4):249-54. doi: 10.1016/j.ejcb.2005.08.003. Epub 2005 Sep 13.
Some RGD-type integrins rely on a synergistic site in addition to the canonical RGD site for ligand binding. However, the precise involvement of each of these recognition sites during cell adhesion is still unclear. Here we review recent investigations on integrin alphaIIbbeta3-mediated cell adhesion to immobilized fibrinogen providing evidence that the fibrinogen synergy gamma(400-411) sequence by itself promotes cell attachment by initiating alphaIIbbeta3 clustering and recruitment of intracellular proteins to focal complexes, while the RGD motif subsequently acts as a molecular switch on the beta3 subunit to induce a conformational change necessary for RhoA activation and full cell spreading.
一些RGD型整合素除了经典的RGD位点外,还依赖一个协同位点来结合配体。然而,这些识别位点在细胞黏附过程中的确切作用仍不清楚。在此,我们综述了近期关于整合素αIIbβ3介导的细胞与固定化纤维蛋白原黏附的研究,这些研究提供了证据表明,纤维蛋白原协同γ(400-411)序列本身通过启动αIIbβ3聚集以及将细胞内蛋白质募集到粘着斑复合物来促进细胞附着,而RGD基序随后作为β3亚基上的分子开关,诱导RhoA激活和细胞完全铺展所必需的构象变化。