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Please use this identifier to cite or link to this item: http://hdl.handle.net/1993/2889

Title: The association of caveolae, actin, and the dystrophin-glycoprotein complex: a role in smooth muscle phenotype and function?
Authors: Halayko, AJ
Stelmack, GL
Keywords: caveolin
dystroglycan
filamin
mechanical plasticity
G-protein-coupled receptors
SARCOGLYCAN-SARCOSPAN COMPLEX
PROTEIN-COUPLED RECEPTOR
LIGHT-CHAIN PHOSPHATASE
SERUM RESPONSE FACTOR
OPERATED CA2+ ENTRY
MAP KINASE CASCADE
VASCULAR SMOOTH
MUSCULAR-DYSTROPHY
MECHANICAL STRAIN
BETA-DYSTROGLYCAN
Issue Date: 31-Oct-2005
Citation: 0008-4212; CAN J PHYSIOL PHARMACOL, OCT 2005, vol. 83, no. 10, p.877 to 891.
Abstract: Smooth muscle cells exhibit phenotypic and mechanical plasticity. During maturation, signalling pathways controlling actin dynamics modulate contractile apparatus-associated gene transcription and contractile apparatus remodelling resulting from length change. Differentiated myocytes accumulate abundant caveolae that evolve from the structural association of lipid rafts with caveolin-1, a protein with domains that confer unique functional properties. Caveolae and caveolin-1 modulate and participate in receptor-mediated signalling, and thus contribute to functional diversity of phenotypically similar myocytes. In mature smooth muscle, caveolae are partitioned into discrete linear domains aligned with structural proteins that tether actin to the extracellular matrix. Caveolin-1 binds with beta-dystroglycan, a subunit of the dystrophin glycoprotein complex (DGC), and with filamin, an actin binding protein that organizes cortical actin, to which integrins and focal adhesion complexes are anchored. The DGC is linked to the actin cytoskeleton by a dystrophin subunit and is a receptor for extracellular laminin. Thus, caveolae and caveolin-associated signalling proteins and receptors are linked via structural proteins to a dynamic filamentous actin network. Despite development of transgenic models to investigate caveolins and membrane-associated actin-linking proteins in skeletal and cardiac muscle function, only superficial understanding of this association in smooth muscle phenotype and function has emerged.
URI: http://hdl.handle.net/1993/2889
Appears in Collection(s):Research Publications (UofM Student, Faculty and Staff only access)

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