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

Grisoni, Karine; Gieseler, Kathrin; Mariol, Marie Christine; Martin, Edwige; Carre-Pierrat, Maïté; Moulder, Gary; Barstead, Robert; Ségalat, Laurent

doi:10.1016/j.jmb.2003.08.021

Cited by 36 publications

(51 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The resulting prey plasmid was transformed into the yeast strain Y187. Interaction between DYC-1S and DYS-1 was assayed as described (Grisoni et al, 2003) A two-hybrid screening was performed as described (Fromont-Racine et al, 1997) by mating CG1945 yeasts transformed with pSEB with Y187 yeasts transformed with a random primed C. elegans cDNA activation domain library (RB2) subcloned into the pACT vector (R. Barstead, Oklahoma Medical Research Foundation, Oklahoma City). Diploid clones, 6.8 ϫ 10 6 , containing the pSEB bait plasmid and one prey-pACT2 plasmid (from the library) were analyzed for their ability to grow on minimal medium lacking Leu, Trp, and His, after 3-d incubation at 30°C.…”

Section: Yeast Two-hybrid Assay and Screeningmentioning

confidence: 99%

“…Interactions between different forms of DYC-1S and ZYX-1 were assayed as described (Grisoni et al, 2003) after mating of transformed CG1945 yeast cells with the transformed Y187 yeast cells. Ten microliters of mating cultures were deposed on minimal medium lacking leucine (Leu), tryptophan (Trp), and histidine (His) and minimal medium lacking Leu and Trp (growth control) and incubated for 3 d at 30°C.…”

Section: Mapping Of Dyc-1-and Zyx-1-interacting Regions By Yeast Two-mentioning

confidence: 99%

“…These mutants undergo only slight muscle degeneration (Bessou et al, 1998;Grisoni et al, 2003). However, in a sensitized hlh-1(cc561) background, which is a mild mutation of the C. elegans homologue of the myogenic factor MyoD, dys-1 mutations lead to an extensive time-dependent muscle degeneration (Gieseler et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

“…Interestingly other genes have been identified whose mutations produce a behavioral phenotype identical to that of dys-1 mutants: dyc-1, dyb-1 (dystrobrevin), stn-1 (syntrophin), dgn-1 (dystroglycan), sgn-1 (sarcoglycan), snf-6 (an acetylcholine transporter) and slo-1 (a potassium channel) (Giesler et al, 2000(Giesler et al, , 2001Grisoni et al, 2002bGrisoni et al, , 2003Kim et al, 2004;Carre-Pierrat et al, 2006). The similarity between the phenotypes suggests that these genes may participate in the same biological function as the C. elegans dys-1 and makes their investigation an important step in understanding dystrophin function in the nematode.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

DYC-1, a Protein Functionally Linked to Dystrophin inCaenorhabditis elegansIs Associated with the Dense Body, Where It Interacts with the Muscle LIM Domain Protein ZYX-1

Lecroisey

Martin

Mariol

et al. 2008

MBoC

Self Cite

View full text Add to dashboard Cite

In Caenorhabditis elegans, mutations of the dystrophin homologue, dys-1, produce a peculiar behavioral phenotype (hyperactivity and a tendency to hypercontract). In a sensitized genetic background, dys-1 mutations also lead to muscle necrosis. The dyc-1 gene was previously identified in a genetic screen because its mutation leads to the same phenotype as dys-1, suggesting that the two genes are functionally linked. Here, we report the detailed characterization of the dyc-1 gene. dyc-1 encodes two isoforms, which are expressed in neurons and muscles. Isoform-specific RNAi experiments show that the absence of the muscle isoform, and not that of the neuronal isoform, is responsible for the dyc-1 mutant phenotype. In the sarcomere, the DYC-1 protein is localized at the edges of the dense body, the nematode muscle adhesion structure where actin filaments are anchored and linked to the sarcolemma. In yeast two-hybrid assays, DYC-1 interacts with ZYX-1, the homologue of the vertebrate focal adhesion LIM domain protein zyxin. ZYX-1 localizes at dense bodies and M-lines as well as in the nucleus of C. elegans striated muscles. The DYC-1 protein possesses a highly conserved 19 amino acid sequence, which is involved in the interaction with ZYX-1 and which is sufficient for addressing DYC-1 to the dense body. Altogether our findings indicate that DYC-1 may be involved in dense body function and stability. This, taken together with the functional link between the C. elegans DYC-1 and DYS-1 proteins, furthermore suggests a requirement of dystrophin function at this structure. As the dense body shares functional similarity with both the vertebrate Z-disk and the costamere, we therefore postulate that disruption of muscle cell adhesion structures might be the primary event of muscle degeneration occurring in the absence of dystrophin, in C. elegans as well as vertebrates.

show abstract

Section: Yeast Two-hybrid Assay and Screeningmentioning

confidence: 99%

Section: Mapping Of Dyc-1-and Zyx-1-interacting Regions By Yeast Two-mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

DYC-1, a Protein Functionally Linked to Dystrophin inCaenorhabditis elegansIs Associated with the Dense Body, Where It Interacts with the Muscle LIM Domain Protein ZYX-1

Lecroisey

Martin

Mariol

et al. 2008

MBoC

Self Cite

View full text Add to dashboard Cite

show abstract

“…Moreover, they also show that the snf-6 transporter binds to the syntrophin protein (stn-1), an anchoring protein that is part of the dystrophin complex in vertebrate and C. elegans muscle. 5 In the absence of either dys-1 or stn-1, snf-6 expression seems reduced.…”

mentioning

confidence: 99%