Isolation and characterization of three distinct cDNAs for the chicken c-ski gene.

Sutrave, P; Hughes, S.H.

doi:10.1128/mcb.9.9.4046

Cited by 50 publications

(78 citation statements)

References 25 publications

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“…1B). Two other species for which c-ski cDNAs have been cloned and sequenced, chicken (Sutrave and Hughes, 1989) and Xenopus (Sleeman and Laskey, 1993), code for exon 1 amino acid sequences that are 80.7 and 74.5% identical to mouse, respectively (Fig. 1B).…”

Section: Cloning Of a Genomic Fragment Of Mouse C-ski Which Encodes Ementioning

confidence: 99%

“…2). Because the exon I region of ski is highly conserved in the related gene, sno, we then chose to use a probe from the 3' non-coding region of c-ski because in the human and chicken mRNAs this region is unre- (Nomura et al, 1989;Sutrave and Hughes, 1989;Boyer et al, 1993). Both of these probes gave the same pattern of in situ hybridization at all developmental stages examined, indicating that the differences observed reflect only changes in c-ski expression.…”

Section: Localization Of Ski Mrnas By In Situ Hybridization Of Mouse mentioning

confidence: 99%

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Enhanced expression of mouse c‐ski accompanies terminal skeletal muscle differentiation in vivo and in vitro

Namciu

Lyons

Micales

et al. 1995

Developmental Dynamics

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Overexpression of either v-ski, or the proto-oncogene, c-ski, in quail embryo fibroblasts induces the expression of myoD and myogenin, converting the cells to myoblasts capable of differentiating into skeletal myotubes. In transgenic mice, overexpression of ski also influences muscle development, but in this case it effects fully formed muscle, causing hypertrophy of fast skeletal muscle fibers. In attempts to determine whether endogenous mouse c-ski plays a role in either early muscle cell determination or late muscle cell differentiation, we analyzed mRNA expression during muscle development in mouse embryos and during in vitro terminal differentiation of skeletal myoblasts. To generate probes for these studies we cloned coding and 3' non-coding regions of mouse c-ski. In situ hybridization revealed low c-ski expression in somites, and only detected elevated levels of mRNA in skeletal muscle beginning at about 12.5 days of gestation. Northern analysis revealed a two-fold increase in c-ski mRNA during terminal differentiation of skeletal muscle cell lines in vitro. Our results suggest that c-ski plays a role in terminal differentiation of skeletal muscle cells not in the determination of cells to the myogenic Lineage. 0 1995 Wiley-Liss, Inc.

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Section: Cloning Of a Genomic Fragment Of Mouse C-ski Which Encodes Ementioning

confidence: 99%

Section: Localization Of Ski Mrnas By In Situ Hybridization Of Mouse mentioning

confidence: 99%

Enhanced expression of mouse c‐ski accompanies terminal skeletal muscle differentiation in vivo and in vitro

Namciu

Lyons

Micales

et al. 1995

Developmental Dynamics

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“…The cellular homologue c-ski has been identi®ed from several species, including human, chicken, and Xenopus (Nomura et al, 1989;Stavnezer et al, 1989;Sutrave and Hughes, 1989;Sleeman and Laskey, 1993). The chicken c-ski proto-oncogene products (c-Ski) are nuclear proteins of 750 amino acids Sutrave and Hughes, 1989;Sutrave et al, 1990a).…”

Section: Introductionmentioning

confidence: 99%

Increased susceptibility to tumorigenesis of ski-deficient heterozygous mice

Shinagawa¹,

Nomura²,

Colmenares

et al. 2001

Oncogene

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“…v-Ski is a truncated form of the c-Ski protein that is missing 20 amino acids from the amino terminus and 292 amino acids from the carboxyl terminus (2)(3)(4). This truncation, which removes a carboxyl-terminal dimerization domain, plays no role in the activation of ski as an oncogene (5,6).…”

mentioning

confidence: 99%

Transcriptional Repression by v-Ski and c-Ski Mediated by a Specific DNA Binding Site

Nicol¹,

Stavnezer²

1998

Journal of Biological Chemistry

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The Ski oncoprotein has been shown to bind DNA and activate transcription in conjunction with other cellular factors. Because tumor cells or myogenic cells were used for those studies, it is not clear that those activities of Ski are related to its transforming ability. In this study, we use a nuclear extract of c-ski-transformed cells to identify a specific DNA binding site for Ski with the consensus sequence GTCTAGAC. We demonstrate that both c-Ski and v-Ski in nuclear extracts are components of complexes that bind specifically to this site. By evaluating the features of the sequence that are critical for binding, we show that binding is cooperative. Although Ski cannot bind to this sequence on its own, we use cross-linking with ultraviolet light to show that Ski binds to this site along with several unidentified cellular proteins. Furthermore, we find that Ski represses transcription either through upstream copies of this element or when brought to the promoter by a heterologous DNA binding domain. This is the first demonstration that Ski acts as a repressor rather than an activator and could provide new insights into regulation of gene expression by Ski.

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Isolation and characterization of three distinct cDNAs for the chicken c-ski gene.

Cited by 50 publications

References 25 publications

Enhanced expression of mouse c‐ski accompanies terminal skeletal muscle differentiation in vivo and in vitro

Enhanced expression of mouse c‐ski accompanies terminal skeletal muscle differentiation in vivo and in vitro

Increased susceptibility to tumorigenesis of ski-deficient heterozygous mice

Transcriptional Repression by v-Ski and c-Ski Mediated by a Specific DNA Binding Site

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