ARAP1: A point of convergence for Arf and Rho signaling

被引：142

作者：

Miura, K

Jacques, KM

Stauffer, S

Kubosaki, A

Zhu, KJ

Hirsch, DS

Resau, J

Zheng, Y

Randazzo, PA ^{[1
]}

机构：

[1] NCI, Cellular Oncol Lab, Bethesda, MD 20892 USA

[2] Natl Inst Dent & Craniofacial Res, Expt Med Sect, Oral Infect & Immun Branch, Bethesda, MD 20892 USA

[3] Univ Tennessee, Ctr Hlth Sci, Dept Mol Sci, Memphis, TN 38163 USA

[4] Van Andel Res Inst, Grand Rapids, MI 49503 USA

来源：

MOLECULAR CELL | 2002年 / 9卷 / 01期

关键词：

D O I：

10.1016/S1097-2765(02)00428-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have identified ARAP1 and ARAP2 and examined ARAP1 as a possible link between phosphoinositide-, Arf-, and Rho-mediated cell signaling. ARAP1 contains Arf GAP, Rho GAP, Ankyrin repeat, Ras-associating, and five PH domains. In vitro, ARAP1 had Rho GAP and phosphatidylinositol (3,4,5) trisphosphate (PIP3)-dependent Arf GAP activity. ARAP1 associated with the Golgi. The Rho GAP activity mediated cell rounding and loss of stress fibers when ARAP1 was overexpressed. The Arf GAP activity mediated changes in the Golgi apparatus and the formation of filopodia, the latter a consequence of increased cellular activity of Cdc42. The Arf GAP and Rho GAP activities both contributed to inhibiting cell spreading. Thus, ARAP1 is a PIP3-dependent Arf GAP that regulates Arf-, Rho-, and Cdc42-dependent cell activities.

引用

收藏

页码：109 / 119

页数：11

相关论文

共 48 条

[21] Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices [J].

Krugmann, S ;

Anderson, KE ;

Ridley, SH ;

Risso, N ;

McGregor, A ;

Coadwell, J ;

Davidson, K ;

Eguinoa, A ;

Ellson, CD ;

Lipp, P ;

Manifava, M ;

Ktistakis, N ;

Painter, G ;

Thuring, JW ;

Cooper, MA ;

Lim, ZY ;

Holmes, AB ;

Dove, SK ;

Michell, RH ;

Grewal, A ;

Nazarian, A ;

Erdjument-Bromage, H ;

Tempst, P ;

Stephens, LR ;

Hawkins, PT .

MOLECULAR CELL, 2002, 9 (01) :95-108

[22] Regulation of receptor-mediated endocytosis by Rho and Rac [J].

Lamaze, C ;

Chuang, TH ;

Terlecky, LJ ;

Bokoch, GM ;

Schmid, SL .

NATURE, 1996, 382 (6587) :177-179

[23] Structural basis of 3-phosphoinositide recognition by pleckstrin homology domains [J].

Lietzke, SE ;

Bose, S ;

Cronin, T ;

Klarlund, J ;

Chawla, A ;

Czech, MP ;

Lambright, DG .

MOLECULAR CELL, 2000, 6 (02) :385-394

[24] PI(4,5)P2 regulation of surface membrane traffic [J].

Martin, TFJ .

CURRENT OPINION IN CELL BIOLOGY, 2001, 13 (04) :493-499

[25]

May RC, 2001, J CELL SCI, V114, P1061

[26] Regulated membrane localization of Tiam1, mediated by the NH2-terminal pleckstrin homology domain, is required for Rac-dependent membrane ruffling and c-jun NH2-terminal kinase activation [J].

Michiels, F ;

Stam, JC ;

Hordijk, PL ;

vanderKammen, RA ;

RuulsVanStalle, L ;

Feltkamp, CA ;

Collard, JG .

JOURNAL OF CELL BIOLOGY, 1997, 137 (02) :387-398

[27] Molecules in the ARF orbit [J].

Moss, J ;

Vaughan, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (34) :21431-21434

[28] cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network [J].

Müsch, A ;

Cohen, D ;

Kreitzer, G ;

Rodriguez-Boulan, E .

EMBO JOURNAL, 2001, 20 (09) :2171-2179

[29] RHO, RAC, AND CDC42 GTPASES REGULATE THE ASSEMBLY OF MULTIMOLECULAR FOCAL COMPLEXES ASSOCIATED WITH ACTIN STRESS FIBERS, LAMELLIPODIA, AND FILOPODIA [J].

NOBES, CD ;

HALL, A .

CELL, 1995, 81 (01) :53-62

[30] ARF1 mediates paxillin recruitment to focal adhesions and potentiates Rho-stimulated stress fiber formation in intact and permeabilized Swiss 3T3 fibroblasts [J].

Norman, JC ;

Jones, D ;

Barry, ST ;

Holt, MR ;

Cockcroft, S ;

Critchley, DR .

JOURNAL OF CELL BIOLOGY, 1998, 143 (07) :1981-1995

← 1 2 3 4 5 →