Connexin Family Members Target to Lipid Raft Domains and Interact with Caveolin-1†

Biochemistry ◽  
2002 ◽  
Vol 41 (18) ◽  
pp. 5754-5764 ◽  
Author(s):  
Anne-Lane Schubert ◽  
William Schubert ◽  
David C. Spray ◽  
Michael P. Lisanti
Keyword(s):  
Lipid Raft ◽  
Family Members ◽  
Caveolin 1 ◽  
Raft Domains

scholarly journals Lipid rafts mediate internalization of β1-integrin in migrating intestinal epithelial cells

2008 ◽  
Vol 295 (5) ◽  
pp. G965-G976 ◽  
Author(s):  
Elena V. Vassilieva ◽  
Kirsten Gerner-Smidt ◽  
Andrei I. Ivanov ◽  
Asma Nusrat
Keyword(s):  
Epithelial Cells ◽  
Lipid Rafts ◽  
Lipid Raft ◽  
Intestinal Epithelial Cells ◽  
Focal Adhesions ◽  
Endocytic Pathway ◽  
Dependent Manner ◽  
Intestinal Epithelial ◽  
Caveolin 1 ◽  
Cell Matrix

Intestinal mucosal inflammation is associated with epithelial wounds that rapidly reseal by migration of intestinal epithelial cells (IECs). Cell migration involves cycles of cell-matrix adhesion/deadhesion that is mediated by dynamic turnover (assembly and disassembly) of integrin-based focal adhesions. Integrin endocytosis appears to be critical for deadhesion of motile cells. However, mechanisms of integrin internalization during remodeling of focal adhesions of migrating IECs are not understood. This study was designed to define the endocytic pathway that mediates internalization of β1-integrin in migrating model IECs. We observed that, in SK-CO15 and T84 colonic epithelial cells, β1-integrin is internalized in a dynamin-dependent manner. Pharmacological inhibition of clathrin-mediated endocytosis or macropinocytosis and small-interfering RNA (siRNA)-mediated knock down of clathrin did not prevent β1-integrin internalization. However, β1-integrin internalization was inhibited following cholesterol extraction and after overexpression of lipid raft protein, caveolin-1. Furthermore, internalized β1-integrin colocalized with the lipid rafts marker cholera toxin, and siRNA-mediated knockdown of caveolin-1 and flotillin-1/2 increased β1-integrin endocytosis. Our data suggest that, in migrating IEC, β1-integrin is internalized via a dynamin-dependent lipid raft-mediated pathway. Such endocytosis is likely to be important for disassembly of integrin-based cell-matrix adhesions and therefore in regulating IEC migration and wound closure.

scholarly journals SCP-2/SCP-x gene ablation alters lipid raft domains in primary cultured mouse hepatocytes

2007 ◽  
Vol 48 (10) ◽  
pp. 2193-2211 ◽  
Author(s):  
Barbara P. Atshaves ◽  
Avery L. McIntosh ◽  
H. Ross Payne ◽  
Adalberto M. Gallegos ◽  
Kerstin Landrock ◽  
...  
Keyword(s):  
Lipid Raft ◽  
Gene Ablation ◽  
Mouse Hepatocytes ◽  
X Gene ◽  
Raft Domains

scholarly journals Flotillin-1-enriched Lipid Raft Domains Accumulate on Maturing Phagosomes

2001 ◽  
Vol 276 (21) ◽  
pp. 18507-18512 ◽  
Author(s):  
Jean-François Dermine ◽  
Sophie Duclos ◽  
Jérome Garin ◽  
François St-Louis ◽  
Shane Rea ◽  
...  
Keyword(s):  
Lipid Raft ◽  
Raft Domains

scholarly journals Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation

2001 ◽  
Vol 154 (4) ◽  
pp. 829-840 ◽  
Author(s):  
Robert T. Watson ◽  
Satoshi Shigematsu ◽  
Shian-Huey Chiang ◽  
Silvia Mora ◽  
Makoto Kanzaki ◽  
...  
Keyword(s):  
Lipid Raft ◽  
Membrane Trafficking ◽  
Glucose Transporter ◽  
Spatial Separation ◽  
Glut4 Translocation ◽  
Insulin Stimulation ◽  
Glut 4 Translocation ◽  
Raft Domains ◽  
Lipid Raft Microdomains ◽  
Stimulation Of

Recent studies indicate that insulin stimulation of glucose transporter (GLUT)4 translocation requires at least two distinct insulin receptor–mediated signals: one leading to the activation of phosphatidylinositol 3 (PI-3) kinase and the other to the activation of the small GTP binding protein TC10. We now demonstrate that TC10 is processed through the secretory membrane trafficking system and localizes to caveolin-enriched lipid raft microdomains. Although insulin activated the wild-type TC10 protein and a TC10/H-Ras chimera that were targeted to lipid raft microdomains, it was unable to activate a TC10/K-Ras chimera that was directed to the nonlipid raft domains. Similarly, only the lipid raft–localized TC10/ H-Ras chimera inhibited GLUT4 translocation, whereas the TC10/K-Ras chimera showed no significant inhibitory activity. Furthermore, disruption of lipid raft microdomains by expression of a dominant-interfering caveolin 3 mutant (Cav3/DGV) inhibited the insulin stimulation of GLUT4 translocation and TC10 lipid raft localization and activation without affecting PI-3 kinase signaling. These data demonstrate that the insulin stimulation of GLUT4 translocation in adipocytes requires the spatial separation and distinct compartmentalization of the PI-3 kinase and TC10 signaling pathways.

scholarly journals Caveolin-1 interacts with a lipid raft-associated population of fatty acid synthase

Cell Cycle ◽  
2008 ◽  
Vol 7 (14) ◽  
pp. 2257-2267 ◽  
Author(s):  
Dolores Di Vizio ◽  
Rosalyn M. Adam ◽  
Jayoung Kim ◽  
Robert Kim ◽  
Federica Sotgia ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Lipid Raft ◽  
Fatty Acid Synthase ◽  
Caveolin 1

scholarly journals 7-Ketocholesterol Incorporation into Sphingolipid/Cholesterol-enriched (Lipid Raft) Domains Is Impaired by Vitamin E

2009 ◽  
Vol 284 (23) ◽  
pp. 15826-15834 ◽  
Author(s):  
Marie-Charlotte Royer ◽  
Stéphanie Lemaire-Ewing ◽  
Catherine Desrumaux ◽  
Serge Monier ◽  
Jean-Paul Pais de Barros ◽  
...  
Keyword(s):  
Vitamin E ◽  
Lipid Raft ◽  
Raft Domains

scholarly journals The Mechanism of Polyplex Internalization into Cells: Testing the GM1/Caveolin-1 Lipid Raft Mediated Endocytosis Pathway

2010 ◽  
Vol 7 (1) ◽  
pp. 267-279 ◽  
Author(s):  
Rong Qi ◽  
Douglas G. Mullen ◽  
James R. Baker ◽  
Mark M. Banaszak Holl
Keyword(s):  
Lipid Raft ◽  
Caveolin 1 ◽  
Endocytosis Pathway

Modeling lipid raft domains containing a mono-unsaturated phosphatidylethanolamine species

RSC Advances ◽  
2015 ◽  
Vol 5 (47) ◽  
pp. 37102-37111 ◽  
Author(s):  
M. Ferraro ◽  
M. Masetti ◽  
M. Recanatini ◽  
A. Cavalli ◽  
G. Bottegoni
Keyword(s):  
Membrane Protein ◽  
Lipid Rafts ◽  
Protein Interactions ◽  
Lipid Raft ◽  
Coarse Grained ◽  
Coarse Grained Model ◽  
Raft Domains

An advanced coarse-grained model for “atypical” lipid rafts was built and validated to be employed in studies of membrane-protein interactions.

Sign in / Sign up

Export Citation Format

Share Document