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Tight Complex Formation between Cosmc Chaperone and Its Specific Client Non-native T-synthase Leads to Enzyme Activity and Client-driven Dissociation
The interaction of the endoplasmic reticulum molecular chaperone Cosmc with its specific client T-synthase (Core 1 β1–3-galactosyltransferase) is required for folding of the enzyme and eventual movement of the T-synthase to the Golgi, but the mechanism of interaction is unclear. Here we show that th...
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| Asıl Yazarlar: | , , |
|---|---|
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Biochemistry and Molecular Biology
2012
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3346102/ https://ncbi.nlm.nih.gov/pubmed/22416136 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.312587 |
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