COMPLEMENTARY DISTRIBUTIONS OF VINCULIN AND DYSTROPHIN DEFINE 2 DISTINCT SARCOLEMMA DOMAINS IN SMOOTH-MUSCLE

被引:141
作者
NORTH, AJ
GALAZKIEWICZ, B
BYERS, TJ
GLENNEY, JR
SMALL, JV
机构
[1] CHILDRENS HOSP MED CTR, HOWARD HUGHES MED INST, BOSTON, MA 02115 USA
[2] HARVARD UNIV, SCH MED, BOSTON, MA 02115 USA
[3] UNIV KENTUCKY, COLL MED, MARKEY CANC CTR, DEPT BIOCHEM, LEXINGTON, KY 40536 USA
关键词
D O I
10.1083/jcb.120.5.1159
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The sarcolemma of the smooth muscle cell displays two alternating structural domains in the electron microscope: densely-staining plaques that correspond to the adherens junctions and intervening uncoated regions which are rich in membrane invaginations, or caveolae. The adherens junctions serve as membrane anchorage sites for the actin cytoskeleton and are typically marked by antibodies to vinculin. We show here by immunofluorescence and immunoelectron microscopy that dystrophin is specifically localized in the caveolae-rich domains of the smooth muscle sarcolemma, together with the caveolae-associated molecule caveolin. Additional labeling experiments revealed that beta1 integrin and fibronectin are confined to the adherens junctions, as indicated by their codistribution with vinculin and tensin. Laminin, on the other hand, is distributed around the entire cell perimeter. The sarcolemma of the smooth muscle cell is thus divided into two distinct domains, featuring different and mutually exclusive components. This simple bipartite domain organization contrasts with the more complex organization of the skeletal muscle sarcolemma: smooth muscle thus offers itself as a useful system for localizing, among other components, potential interacting partners of dystrophin.
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页码:1159 / 1167
页数:9
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