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Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells."

Caveolins muscle their way into the regulation of cell differentiation, development, and... Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells." Rennolds S Ostrom Department of Pharmacology and the Vascular Biology Center of Excellence, University of Tennessee Health Science Center, Memphis, Tennessee SINCE THEIR INITIAL CHARACTERIZATION in the early 1990s, the functions ascribed to caveolin proteins have steadily increased in complexity and sophistication. Caveolins were initially identified as the main component of the "coat" of caveolae, vesicles that were originally described in the 1950s ( 22 ). Caveolae were initially considered to be vesicular structures that mediated transcytosis of macromolecules; caveolins were thus viewed as structural proteins that aided formation of the vesicle. By the mid-1990s, caveolae and their "siblings," lipid rafts, rapidly became appreciated as "hot spots" for plasmalemmal signaling, with a newly recognized function as organizational or scaffolding proteins that attract and retain certain signaling moieties in efficient complexes. However, in recent years, evidence has steadily mounted to support the notion that caveolins are much more than simply structural components of vesicles or docking sites for signaling molecules. In fact, caveolins are now acknowledged to be critical http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells."

Ostrom, Rennolds S
AJP - Cell Physiology , Volume 288 (3): C507 – Mar 1, 2005
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References (39)

Publisher
The American Physiological Society
Copyright
Copyright © 2010 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
DOI
10.1152/ajpcell.00531.2004
pmid
15692149
Publisher site
See Article on Publisher Site

Abstract

Caveolins muscle their way into the regulation of cell differentiation, development, and function. Focus on "Muscle-specific interaction of caveolin isoforms: differential complex formation between caveolins in fibroblastic vs. muscle cells." Rennolds S Ostrom Department of Pharmacology and the Vascular Biology Center of Excellence, University of Tennessee Health Science Center, Memphis, Tennessee SINCE THEIR INITIAL CHARACTERIZATION in the early 1990s, the functions ascribed to caveolin proteins have steadily increased in complexity and sophistication. Caveolins were initially identified as the main component of the "coat" of caveolae, vesicles that were originally described in the 1950s ( 22 ). Caveolae were initially considered to be vesicular structures that mediated transcytosis of macromolecules; caveolins were thus viewed as structural proteins that aided formation of the vesicle. By the mid-1990s, caveolae and their "siblings," lipid rafts, rapidly became appreciated as "hot spots" for plasmalemmal signaling, with a newly recognized function as organizational or scaffolding proteins that attract and retain certain signaling moieties in efficient complexes. However, in recent years, evidence has steadily mounted to support the notion that caveolins are much more than simply structural components of vesicles or docking sites for signaling molecules. In fact, caveolins are now acknowledged to be critical

Journal

AJP - Cell Physiology – The American Physiological Society

Published: Mar 1, 2005

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