Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

Ibraghimov‐Beskrovnaya, Oxana; Ervasti, James M.; Leveille, Cynthia J.; Slaughter, Clive A.; Sernett, Suzanne W.; Campbell, Kevin P.

doi:10.1038/355696a0

Cited by 1,278 publications

(1,018 citation statements)

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“…The characterization of different dystrophin-associated protein complexes (DAPCs), such as those localized in the skeletal muscle, neuromuscular junction, brain, lung, retina and kidney, has been reported [3,[11][12][13]17,32]. In addition, an increasing number of cellular functions associated with these multiple protein complexes have been proposed, such as membrane stability, cellular signaling and force transduction [7,33,34].…”

Section: Discussionmentioning

confidence: 99%

“…Proteins that comprise the DAPC are structurally organized into three distinct subcomplexes: the cytoskeletal proteins dystrophin, dystrobrevins (α and β subunits) and syntrophins (α, β and γ subunits); the dystroglycans (α and β subunits); and the sarcoglycans (α, β, γ, δ and ε subunits). In skeletal muscle, the DAPC is assembled around dystrophin; this scaffold links the actin cytoskeleton to the basement membrane via the transmembrane protein βdystroglycan and anchors the syntrophins and dystrobrevins to the muscle membrane [2,3]. Loss of dystrophin leads to disassembly of the complex and muscle degeneration [3].It has been shown that neuronal nitric oxide synthase (nNOS) binds to skeletal muscle syntrophin through PDZ domain interactions [4]; thus, the DAPC may also regulate signal transduction.…”

Section: Introductionmentioning

confidence: 99%

“…In skeletal muscle, the DAPC is assembled around dystrophin; this scaffold links the actin cytoskeleton to the basement membrane via the transmembrane protein βdystroglycan and anchors the syntrophins and dystrobrevins to the muscle membrane [2,3]. Loss of dystrophin leads to disassembly of the complex and muscle degeneration [3].It has been shown that neuronal nitric oxide synthase (nNOS) binds to skeletal muscle syntrophin through PDZ domain interactions [4]; thus, the DAPC may also regulate signal transduction. Many of the DAPC components found in skeletal muscle, including β-and ε-sarcoglycans, dystroglycans and syntrophins, are also expressed in other tissues [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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, et al.. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix.. Experimental Cell Research, Elsevier, 2006, 312 (16) ABSTRACT: Dystrophin is an essential component in the assembly and maintenance of the dystrophinassociated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, β-sarcoglycan, β-dystroglycan, α-and β-syntrophin, α1-and β-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by coimmunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, β-dystroglycan, nNOS, β-sarcoglycan, α/β syntrophin, α1-dystrobrevin and β-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, β-dystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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“…Dystroglycan (Dg) is a membrane-spanning cell adhesion receptor encoded by a single gene whose product is cleaved posttranslationally to yield the mature two-chain form, ␣-Dg and ␤-Dg (Ibraghimov-Beskrovnaya et al, 1992). The ␤-Dg modulates signal transduction, acting as a scaffold for the extracellular-signal-related kinase-mitogenactivated protein (ERK-MAP) kinase cascade (Spence et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

In vivo analyzes of dystroglycan function during somitogenesis in Xenopus laevis

Hidalgo

Sirour

Bello

et al. 2008

Developmental Dynamics

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Dystroglycan (Dg) is a cell adhesion receptor for laminin that has been reported to play a role in skeletal muscle cell stability, cytoskeletal organization, cell polarity, and signaling. Here we show that Dg is expressed at both the notochord/somite and the intersomitic boundaries, where laminin and fibronectin are accumulated during somitogenesis. Inhibition of Dg function with morpholino antisense oligonucleotides or a dominant negative mutant results in the normal segmentation of the presomitic mesoderm but affects the number, the size, and the integrity of somites. Depletion of Dg disrupts proliferation and alignment of myoblasts without affecting XMyoD and XMRF4 expression. It also leads to defects in laminin deposition at the intersomitic junctions, whereas expression of integrin ␤1 subunits and fibronectin assembly occur normally. Our results show that Dg is critical for both proliferation and elongation of somitic cells and that the Dg-cytoplasmic domain is required for the laminin assembly at the intersomitic boundaries.

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“…Dystroglycan (DG) is an ubiquitous membrane glycoprotein complex that includes two subunits, a-DG and b-DG, held together by noncovalent interactions (1).…”

Section: Introductionmentioning

confidence: 99%

Enzymatic processing by MMP‐2 and MMP‐9 of wild‐type and mutated mouse β‐dystroglycan

et al. 2012

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SummaryDystroglycan (DG) is a membrane-associated protein complex formed by two noncovalently linked subunits, a-DG, a highly glycosylated extracellular protein, and b-DG, a transmembrane protein. The interface between the two DG subunits, which is crucial to maintain the integrity of the plasma membrane, involves the C-terminal domain of a-DG and the N-terminal extracellular domain of b-DG. It is well known that under both, physiological and pathological conditions, gelatinases (i.e. MMP-9 and/or MMP-2) can degrade DG, disrupting the connection between the extracellular matrix and the cytoskeleton. However, the molecular mechanisms and the exact cleavage sites underlying these events are still largely unknown. In a previous study, we have characterized the enzymatic digestion of the murine b-DG ectodomain by gelatinases, identifying a main cleavage site on the b-DG ectodomain produced by MMP-9. In this article, we have deepened the pattern of the b-DG ectodomain digestion by MMP-2 by using a combined approach based on SDS-PAGE, Orbitrap, and HPLC-ESI-IT mass spectrometry. Furthermore, we have characterized the kinetic parameters of the digestion of some b-DG ectodomain mutants by gelatinases.2012 IUBMB IUBMB Life, 64(12): 988-994, 2012

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Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

Cited by 1,278 publications

References 35 publications

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

In vivo analyzes of dystroglycan function during somitogenesis in Xenopus laevis

Enzymatic processing by MMP‐2 and MMP‐9 of wild‐type and mutated mouse β‐dystroglycan

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