Dystrophin as a focal adhesion protein

Kramarcy, Neal R.; Sealock, Robert

doi:10.1016/0014-5793(90)81356-s

Cited by 40 publications

(1 citation statement)

References 20 publications

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“…If this is the case, the sarcoglycan complex could also be viewed as two distinct but interrelated functional subunits. In support of this hypothesis, the DGC has been linked with other focal adhesion assembly proteins such as integrins ( Kramarcy and Sealock, 1990 ; Lakonishok et al, 1992 ; Yoshida et al, 1998 ) and suggested to function analogously to the integrins as a mechanochemical transducer in skeletal muscle ( Brown and Lucy, 1993 ). Recently, an ecto-ATPase activity has been associated with α-sarcoglycan ( Salviati et al, 1997 ).…”

Section: Discussionmentioning

confidence: 89%

Molecular Organization of Sarcoglycan Complex in Mouse Myotubes in Culture

Chan

Bönnemann

Lidov

et al. 1998

The Journal of Cell Biology

120

135

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The sarcoglycans are a complex of four transmembrane proteins (α, β, γ, and δ) which are primarily expressed in skeletal muscle and are closely associated with dystrophin and the dystroglycans in the muscle membrane. Mutations in the sarcoglycans are responsible for four autosomal recessive forms of muscular dystrophy. The function and the organization of the sarcoglycan complex are unknown. We have used coimmunoprecipitation and in vivo cross-linking techniques to analyze the sarcoglycan complex in cultured mouse myotubes. We demonstrate that the interaction between β- and δ-sarcoglycan is resistant to high concentrations of SDS and α-sarcoglycan is less tightly associated with other members of the complex. Cross-linking experiments show that β-, γ-, and δ-sarcoglycan are in close proximity to one another and that δ-sarcoglycan can be cross-linked to the dystroglycan complex. In addition, three of the sarcoglycans (β, γ, and δ) are shown to form intramolecular disulfide bonds. These studies further our knowledge of the structure of the sarcoglycan complex. Our proposed model of their interactions helps to explain some of the emerging data on the consequences of mutations in the individual sarcoglycans, their effect on the complex, and potentially the clinical course of muscular dystrophies.

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Section: Discussionmentioning

confidence: 89%

Molecular Organization of Sarcoglycan Complex in Mouse Myotubes in Culture

Chan

Bönnemann

Lidov

et al. 1998

The Journal of Cell Biology

120

135

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Utrophin-dystroglycan complex in membranes of adherent cultured cells

James¹,

Mân²,

Wise

et al. 1996

Cell Motil. Cytoskeleton

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In skeletal muscle, dystrophin binds to an oligomeric, transmembrane complex (DAGc; dystrophin‐associated glycoprotein complex) which interacts with laminin in the extracellular matrix. We now present biochemical evidence for an association between utrophin (dystrophin‐related protein, DRP) and a major DAGc component, β‐dystroglycan (43DAG) in cultured cell lines which contain little if any dystrophin. We have shown also that utrophin and β‐dystroglycan co‐localise at or near the plasma membrane and that they co‐sediment in large complexes on sucrose density gradients. On the lower plasma membrane, in contact with the substratum, part of the utrophin and β‐dystroglycan staining co‐localised with α‐actinin in a punctate distribution outside classical vinculin‐rich focal adhesions. β‐dystroglycan, utrophin, syntrophin (59DAP), and α‐actinin were found in all adhesion‐competent cell lines studied, but levels of the last three proteins were greatly reduced in myeloma cells, which cannot readily attach to substrata. Possible roles for utrophin in cultured cells are considered in the light of recent evidence for involvement of utrophin‐glycoprotein complexes in muscle in signal transduction and recruitment of acetylcholine receptors to neuromuscular junctions. © 1996 Wiley‐Liss, Inc.

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