Characterization of the dystrophin‐syntrophin interaction using the two‐hybrid system in yeast

Castelló, Anna; Brocheriou, Valérie; Chafey, Philippe; Kahn, Axel; Gilgenkrantz, Hélène

doi:10.1016/0014-5793(96)00214-1

Cited by 16 publications

(12 citation statements)

References 22 publications

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“…31 The physical interaction between mammalian syntrophin and dystrophin has been demonstrated by a variety of methods, including overlay assay, in vitro binding and immunoprecipitation, and yeast two-hybrid assay. 17,18,34,35 In contrast, despite earlier evidence that C. elegans syntrophin and dystrophin bind to each other in in vitro pulldown experiments, 19 we were not able to show any interaction in the yeast two-hybrid assay, which is considered to be closer to the in vivo situation than in vitro experiments are. The two-hybrid result is in accordance with the absence of a clear syntrophin binding site (as defined by Newey and colleagues 31 ) on the C. elegans dystrophin sequence.…”

Section: Discussioncontrasting

confidence: 81%

The stn-1 Syntrophin Gene of C.elegans is Functionally Related to Dystrophin and Dystrobrevin

Grisoni

Gieseler

Mariol

et al. 2003

Journal of Molecular Biology

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Section: Discussioncontrasting

confidence: 81%

The stn-1 Syntrophin Gene of C.elegans is Functionally Related to Dystrophin and Dystrobrevin

Grisoni

Gieseler

Mariol

et al. 2003

Journal of Molecular Biology

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“…Therefore, the mechanical and nonmechanical defects that arise in muscular dystrophy may occur in part from the loss of these proteins. Dystrophin and the syntrophins, the cytoplasmic components of the DGC, can directly interact (Adams et al, 1993;Ahn and Kunkel, 1995;Ahn et al, 1994;Castello et al, 1996;Peters et al, 1997;Suzuki et al, 1994Suzuki et al, , 1995Yang et al, 1995). Syntrophin interacts with a number of other elements including nitric oxide synthase (Hashida-Okumura et al, 1999;Venema et al, 1997), voltage gated sodium channels (Gee et al, 1998;Schultz et al, 1998), stress activated protein kinase-3 (Hasegawa et al, 1999), caveolin via NOS (Venema et al, 1997), calmodulin , and phosphatidylinositol 4,5-bisphosphate (Venema et al, 1997).…”

Section: Membrane-cytoskeletal-extracellular Matrixmentioning

confidence: 99%

Sarcoglycans in muscular dystrophy

Hack

Groh

McNally

2000

Microsc. Res. Tech.

134

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Muscular dystrophy is a heterogeneous genetic disease that affects skeletal and cardiac muscle. The genetic defects associated with muscular dystrophy include mutations in dystrophin and its associated glycoproteins, the sarcoglycans. Furthermore, defects in dystrophin have been shown to cause a disruption of the normal expression and localization of the sarcoglycan complex. Thus, abnormalities of sarcoglycan are a common molecular feature in a number of dystrophies. By combining biochemistry, molecular cell biology, and human and mouse genetics, a growing understanding of the sarcoglycan complex is emerging. Sarcoglycan appears to be an important, independent mediator of dystrophic pathology in both skeletal muscle and heart. The absence of sarcoglycan leads to alterations of membrane permeability and apoptosis, two shared features of a number of dystrophies. β‐sarcoglycan and δ‐sarcoglycan may form the core of the sarcoglycan subcomplex with α‐ and γ‐sarcoglycan less tightly associated to this core. The relationship of ϵ‐sarcoglycan to the dystrophin‐glycoprotein complex remains unclear. Animals lacking α‐, γ‐ and δ‐sarcoglycan have been described and provide excellent opportunities for further investigation of the function of sarcoglycan. Dystrophin with dystroglycan and laminin may be a mechanical link between the actin cytoskeleton and the extracellular matrix. By positioning itself in close proximity to dystrophin and dystroglycan, sarcoglycan may function to couple mechanical and chemical signals in striated muscle. Sarcoglycan may be an independent signaling or regulatory module whose position in the membrane is determined by dystrophin but whose function is carried out independent of the dystrophin‐dystroglycan‐laminin axis. Microsc. Res. Tech. 48:167–180, 2000. © 2000 Wiley‐Liss, Inc.

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“…Previous studies have shown that these domains are sufficient to mediate the physical interaction between the two proteins and that this interaction likely takes place between the first helices (H1) of each protein [6]. The protein region directly upstream of H1 in both dystrophin and dystrobrevin long isoforms is thought to associate with syntrophins [6,7].…”

Section: Introductionmentioning

confidence: 99%

In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin

1999

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Dystrophin, the product of the gene mutated in Duchenne muscular dystrophy (DMD) is bound by its Cterminus to a protein complex including the related protein dystrobrevin. Both proteins contain a putative coiled-coil domain consisting of two K K-helices. It has been reported that the two proteins bind to each other by the first one of the two K K-helices. We have revisited this question using the Caenorhabditis elegans homologs of dystrophin and dystrobrevin. In vitro interaction occurs through the more conserved second helix. We propose a new model of dystrophin interactions with associated proteins.z 1999 Federation of European Biochemical Societies.

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Characterization of the dystrophin‐syntrophin interaction using the two‐hybrid system in yeast

Cited by 16 publications

References 22 publications

The stn-1 Syntrophin Gene of C.elegans is Functionally Related to Dystrophin and Dystrobrevin

The stn-1 Syntrophin Gene of C.elegans is Functionally Related to Dystrophin and Dystrobrevin

Sarcoglycans in muscular dystrophy

In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin

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