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A single E726Q mutation in the membrane proximal α-helix of integrin β3 subunit induces membrane blebbing by disrupting the membrane-actin cortex interaction / 中国实验血液学杂志
Journal of Experimental Hematology ; (6): 1450-1455, 2011.
Artículo en Chino | WPRIM | ID: wpr-331056
ABSTRACT
The membrane proximal α helix of integrin β subunit cytoplasmic tails plays an important functional role by interacting with various intracellular proteins, namely talin, α-actinin or skelemin. This study was designed to investigate the functional role of 5 highly conserved charged amino acids (R(724), K(725), E(726), E(731), E(733)) within this α helix by site-directed mutagenesis. The result showed that CHO cells expressing the αIIbβ3E726Q mutant had the most prominent phenotype and characterized by defective cell spreading on immobilized fibrinogen. In addition, this E726Q mutation induced membrane blebbing in cells adherent on fibrinogen, and this blebbing could be inhibited by the myosin light chain ATPase inhibitor blebbistatin. It is concluded that the membrane proximal α-helix of integrin β3 subunit is important in linking the phospholipid membrane to the submembraneous actin cortex.
Asunto(s)
Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Química / Mutagénesis Sitio-Dirigida / Cricetulus / Células CHO / Estructura Terciaria de Proteína / Extensiones de la Superficie Celular / Integrina beta3 / Genética / Compuestos Heterocíclicos de 4 o más Anillos / Mutación Límite: Animales Idioma: Chino Revista: Journal of Experimental Hematology Año: 2011 Tipo del documento: Artículo

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Texto completo: Disponible Índice: WPRIM (Pacífico Occidental) Asunto principal: Química / Mutagénesis Sitio-Dirigida / Cricetulus / Células CHO / Estructura Terciaria de Proteína / Extensiones de la Superficie Celular / Integrina beta3 / Genética / Compuestos Heterocíclicos de 4 o más Anillos / Mutación Límite: Animales Idioma: Chino Revista: Journal of Experimental Hematology Año: 2011 Tipo del documento: Artículo