STIMULATION OF HUMAN MONOCYTES WITH MACROPHAGE-COLONY-STIMULATING FACTOR INDUCES A GRB2-MEDIATED ASSOCIATION OF THE FOCAL ADHESION KINASE PP125(FAK) AND DYNAMIN

被引：73

作者：

KHARBANDA, S ^{[1
]}

SALEEM, A ^{[1
]}

YUAN, ZM ^{[1
]}

EMOTO, Y ^{[1
]}

PRASAD, KVS ^{[1
]}

KUFE, D ^{[1
]}

机构：

[1] HARVARD UNIV, SCH MED, DANA FARBER CANC INST, DIV TUMOR IMMUNOL, BOSTON, MA 02115 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 13期

关键词：

D O I：

10.1073/pnas.92.13.6132

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Macrophage colony-stimulating factor (M-CSF) is required for the growth and differentiation of mononuclear phagocytes, In the present studies using human monocytes, we show that M-CSF induces interaction of the Grb2 adaptor protein with the focal adhesion kinase pp125(FAK). The results demonstrate that tyrosine-phosphorylated pp125(FAK) directly interacts with the SH2 domain of Grb2. The findings indicate that a pYENV site at Tyr-925 in pp125(FAK) is responsible for this interaction. We also demonstrate that the Grb2-FAK complex associates with the GTPase dynamin. Dynamin interacts with the SH3 domains of Grb2 and exhibits M-CSF-dependent tyrosine phosphorylation in association with pp125(FAK). These findings suggest that M-CSF-induced signaling involves independent Grb2-mediated pathways, one leading to Ras activation and another involving pp125(FAK) and a GTPase implicated in receptor internalization.

引用

页码：6132 / 6136

页数：5

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