ArticleThe Journal of cell biology1993
Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 159 citations in OpenAlex.
- Smooth muscle ultrastructure - still shrouded in mystery?Protoplasma · 2026Review
- Membrane adhesion junctions regulate airway smooth muscle phenotype and function.Physiological reviews · 2023Review
- Contractile apparatus in CNS capillary pericytes.Neurophotonics · 2022Review
- Reduction of acetylcholine in the hippocampus of hippocampal cholinergic neurostimulating peptide precursor protein knockout mice.Scientific reports · 2021Article
- Contribution of TRPC Channels to Intracellular CaFrontiers in physiology · 2020Article
- Costameres, dense plaques and podosomes: the cell matrix adhesions in cardiovascular mechanosensing.Journal of muscle research and cell motility · 2019Review
- Characterization of a Dmd (EGFP) reporter mouse as a tool to investigate dystrophin expression.Skeletal muscle · 2016Article
- The Sarcoglycan complex is expressed in the cerebrovascular system and is specifically regulated by astroglial Cx30 channels.Frontiers in cellular neuroscience · 2015Article
- Smooth muscle-protein translocation and tissue function.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- The integrin adhesome: from genes and proteins to human disease.Nature reviews. Molecular cell biology · 2014Review
- Vinculin phosphorylation at Tyr1065 regulates vinculin conformation and tension development in airway smooth muscle tissues.The Journal of biological chemistry · 2014Article
- Article
- Astrocytes require insulin-like growth factor I to protect neurons against oxidative injury.F1000Research · 2014Article
- Sparing of muscle mass and function by passive loading in an experimental intensive care unit model.The Journal of physiology · 2013Article
- Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus.Journal of muscle research and cell motility · 2012Review
- Activation of vinculin induced by cholinergic stimulation regulates contraction of tracheal smooth muscle tissue.The Journal of biological chemistry · 2011Article
- N-cadherin cell-cell adhesion complexes are regulated by fibronectin matrix assembly.The Journal of biological chemistry · 2011Article
- Combined extrinsic and intrinsic manipulations exert complementary neuronal enrichment in embryonic rat neural precursor cultures: an in vitro and in vivo analysis.The Journal of comparative neurology · 2009Article
- Airway smooth muscle dynamics: a common pathway of airway obstruction in asthma.The European respiratory journal · 2007Review
- Domain architecture of the smooth-muscle plasma membrane: regulation by annexins.The Biochemical journal · 2005Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 beta 1 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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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.