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Published 11 September 2006. doi:10.1083/jcb.200603111
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 6, 877-888
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Article

RLIP76 (RalBP1) is an R-Ras effector that mediates adhesion-dependent Rac activation and cell migration



Lawrence E. Goldfinger1,2, Celeste Ptak3, Erin D. Jeffery3, Jeffrey Shabanowitz3, Donald F. Hunt3,4, and Mark H. Ginsberg1,2

1 Division of Rheumatology and 2 Division of Hematology-Oncology, Department of Medicine, University of California, San Diego, La Jolla, CA 92093
3 Department of Chemistry and 4 Department of Pathology, University of Virginia, Charlottesville, VA 22904

Correspondence to Mark H. Ginsberg: mhginsberg{at}ucsd.edu

The Ras family of small GTPases regulates cell proliferation, spreading, migration and apoptosis, and malignant transformation by binding to several protein effectors. One such GTPase, R-Ras, plays distinct roles in each of these processes, but to date, identified R-Ras effectors were shared with other Ras family members (e.g., H-Ras). We utilized a new database of Ras-interacting proteins to identify RLIP76 (RalBP1) as a novel R-Ras effector. RLIP76 binds directly to R-Ras in a GTP-dependent manner, but does not physically associate with the closely related paralogues H-Ras and Rap1A. RLIP76 is required for adhesion-induced Rac activation and the resulting cell spreading and migration, as well as for the ability of R-Ras to enhance these functions. RLIP76 regulates Rac activity through the adhesion-induced activation of Arf6 GTPase and activation of Arf6 bypasses the requirement for RLIP76 in Rac activation and cell spreading. Thus, we identify a novel R-Ras effector, RLIP76, which links R-Ras to adhesion-induced Rac activation through a GTPase cascade that mediates cell spreading and migration.

C. Ptak's present address is Advion BioSciences, Inc., Ithaca, NY 14850.

Abbreviations used in this paper: GAP, GTPase-activating protein; GEF, guanine nucleotide exchange factor; RBD, Ral- or Ras-binding domain; TAP, tandem affinity purification; TEVCB, TEV protease cell lysis buffer.


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