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Integrins Regulate Rac Targeting by Internalization of Membrane Domains
Abstract
Translocation of the small GTP-binding protein Rac1 to the cell plasma membrane is essential for activating downstream effectors and requires integrin-mediated adhesion of cells to extracellular matrix. We report that active Rac1 binds preferentially to low-density, cholesterol-rich membranes, and specificity is determined at least in part by membrane lipids. Cell detachment triggered internalization of plasma membrane cholesterol and lipid raft markers. Preventing internalization maintained Rac1 membrane targeting and effector activation in nonadherent cells. Regulation of lipid rafts by integrin signals may regulate the location of membrane domains such as lipid rafts and thereby control domain-specific signaling events in anchorage-dependent cells.
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In the citing paper
“Rho GTPases associate with effector proteins at the cell plasma membrane, including lipid rafts.11–15”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [14]
In the citing paper
“Detachment of cells induces the internalization of lipid rafts, which inhibits the membrane localization of Rac1.”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [14]
In the citing paper
“Active GTP-bound Rac proteins are localized in plasma membrane domains, such as lipid rafts, to associate and activate downstream effector proteins.14,24,38,39”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [14]
In the citing paper
“This detachment-induced Rac dissociation is independent of its activation status.14,15,24”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [14]
In the citing paper
“In detached fibroblasts, Rac is dissociated from the plasma membrane by lipid raft internalization mediated via caveolin phosphorylation and remains in the cytoplasm bound to Rho guanine nucleotide dissociation inhibitor (RhoGDI).”
From Cross-talk between RhoH and Rac1 in regulation of actin cytoskeleton and chemotaxis of hematopoietic progenitor cells (2008) · cites this paper as [14]
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Research works printed but not linked: 22
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“Integrin localization in LRs has a clear meaning in the cancer context [21], as it directs the localization and local activity of potent drivers of tumor progression, such as the small GTPase Rac1 [10, 22, 23].”
Metadata
- Authors
- del Pozo, M. A., Alderson, N. B., Kiosses, W. B., Chiang, H.-H., Anderson, R. G. W., & Schwartz, M. A.
- Affiliations
- Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
- Venue
- Science
- Published
- 2004-02-06
- Volume
- 303
- Issue
- 5659
- Pages
- 839-842
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 475
- References
- 0
- Language
- en
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