دورية أكاديمية
Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase. Evidence for interaction of the N-terminal domain of Stt3p with the protein kinase C cascade.
| العنوان: | Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase. Evidence for interaction of the N-terminal domain of Stt3p with the protein kinase C cascade. |
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| المؤلفون: | Chavan M; Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794, USA., Rekowicz M, Lennarz W |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2003 Dec 19; Vol. 278 (51), pp. 51441-7. Date of Electronic Publication: 2003 Oct 06. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Saccharomyces cerevisiae Proteins*, Hexosyltransferases/*chemistry , Membrane Proteins/*chemistry, Fungal Proteins/genetics ; Fungal Proteins/physiology ; Hexosyltransferases/genetics ; Membrane Proteins/physiology ; Mutation ; Phenotype ; Protein Kinase C/metabolism ; Protein Structure, Tertiary ; Protein Subunits/genetics ; Signal Transduction ; Staurosporine/pharmacology ; Temperature ; Yeasts/enzymology ; Yeasts/growth & development |
| مستخلص: | Over a decade ago, the gene STT3 was identified in a staurosporine and temperature sensitivity screen of yeast. Subsequently the product of this gene was shown to be a subunit of the endoplasmic reticulum-localized oligosaccharyl transferase (OT) complex. Although stt3 mutants are known to be staurosporine-sensitive, we found that mutants of other OT subunits (except ost4 Delta) are staurosporine-resistant, which indicates that this phenotype of stt3 mutants is not simply a consequence of their defect in glycosylation, as previously speculated. Staurosporine sensitivity was found to be an allele-specific phenotype restricted to cells harboring mutations in highly conserved residues in the N-terminal domain of the STT3 protein. Cells bearing mutations in one of the cytosolic-oriented loops (amino acids 158-168) in the N terminus of Stt3p were found to be specifically susceptible to staurosporine. Staurosporine is a specific inhibitor of Pkc1p, and a genetic link had previously been suggested between PKC1 and STT3. It is known that overexpression of PKC1 suppresses the staurosporine sensitivity of the stt3 mutants in an allele-specific manner, which is typical of mutants of Pkc1p cascade. It has been shown that the pkc1 null mutant exhibits lowered OT activity. Our results combined with these previous observations indicate that the N-terminal domain of Stt3p may interact with members of the Pkc1p cascade and consequently mutations in this domain result in staurosporine sensitivity. We further speculate that the Pkc1p regulates OT activity through the N-terminal domain of Stt3p, the C-terminal domain of which possesses the recognition and/or catalytic site of the OT complex. |
| معلومات مُعتمدة: | GM33185 United States GM NIGMS NIH HHS |
| المشرفين على المادة: | 0 (Fungal Proteins) 0 (Membrane Proteins) 0 (Protein Subunits) 0 (Saccharomyces cerevisiae Proteins) EC 2.4.1.- (Hexosyltransferases) EC 2.4.99.18 (STT3 protein, S cerevisiae) EC 2.4.99.18 (dolichyl-diphosphooligosaccharide - protein glycotransferase) EC 2.7.11.13 (Protein Kinase C) H88EPA0A3N (Staurosporine) |
| تواريخ الأحداث: | Date Created: 20031008 Date Completed: 20040130 Latest Revision: 20210209 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1074/jbc.M310456200 |
| PMID: | 14530272 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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| DOI: | 10.1074/jbc.M310456200 |