Cell migration: GAPs between membrane traffic and the cytoskeleton
Open Access
- 1 April 2001
- journal article
- review article
- Published by Springer Nature in EMBO Reports
- Vol. 2 (4) , 277-281
- https://doi.org/10.1093/embo-reports/kve072
Abstract
During cell migration, coordination between membrane traffic, cell substrate adhesion and actin reorganization is required for protrusive activity to occur at the leading edge. Actin organization is regulated by Rho family GTPases and, with a contribution from the endocytic cycle, serves to extend the cell front. The details of the molecular mechanisms that direct membrane traffic at sites of adhesion and rearrange actin at the cell edge are still unknown. However, recent findings show that a number of multi‐domain proteins characterized by an ArfGAP domain interact with both actin‐regulating and integrin‐binding proteins, as well as affecting Rac‐mediated protrusive activity and cell migration. Some of these proteins have been shown to localize to endocytic compartments and to have a role in regulating endocytosis. Given the participation of Arf proteins in regulating membrane traffic, one appealing hypothesis is that the ArfGAPs act as molecular devices that coordinate membrane traffic and cytoskeletal reorganization during cell motility.Keywords
This publication has 43 references indexed in Scilit:
- Acaps Are Arf6 Gtpase-Activating Proteins That Function in the Cell PeripheryThe Journal of cell biology, 2000
- αPIX nucleotide exchange factor is activated by interaction with phosphatidylinositol 3-kinaseOncogene, 1999
- A Tyrosine-phosphorylated Protein That Binds to an Important Regulatory Region on the Cool Family of p21-activated Kinase-binding ProteinsJournal of Biological Chemistry, 1999
- Snapshots of ARF1Cell, 1999
- αPix Stimulates p21-activated Kinase Activity through Exchange Factor-dependent and -independent MechanismsJournal of Biological Chemistry, 1999
- ARF6 Targets Recycling Vesicles to the Plasma Membrane: Insights from an Ultrastructural InvestigationThe Journal of cell biology, 1998
- Cloning of a SH3 Domain-Containing Proline-Rich Protein, p85SPR, and Its Localization in Focal AdhesionBiochemical and Biophysical Research Communications, 1997
- Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodiaCell, 1995
- The small GTP-binding protein rac regulates growth factor-induced membrane rufflingCell, 1992
- Paxillin: a new vinculin-binding protein present in focal adhesions.The Journal of cell biology, 1990