作者: Peter D. Burbelo , Shingo Miyamoto , Atsushi Utani , Suzanne Brill , Kenneth M. Yamada
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摘要: Abstract p120 forms distinct complexes with two phosphoproteins, p62 and p190. Here we have cloned a cDNA encoding protein 51% amino acid identity to p190 (hereafter designated p190-A) it p190-B. The N-terminal portion of p190-B contained several motifs characteristic GTPase domain, while its C terminus Rho GAP domain. A recombinant domain polypeptide showed activity for RhoA, Rac1, G25K/CDC42Hs. Immunoprecipitation immunofluorescence studies demonstrated that was expressed in variety cells localized diffusely the cytoplasm fibrillar patterns co-localized α5β1 integrin receptor fibronectin. Adhesion fibronectin-coated latex beads resulted recruitment significant amounts plasma membrane beneath site bead binding. In contrast, coated polylysine or concanavalin were unable recruit Rho. Additionally, anti-β1 anti-α5 antibody-coated also able large These results identify novel second member family establish existence transmembrane link between integrins new