Difference between revisions of "YGL047W"
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Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived. | Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived. | ||
− | Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation <ref> Averbeck et al., | + | Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation <ref> Averbeck et al., (2008) Alg13p, the catalytic subunit of the endoplasmic reticulum UDP-GlcNAc glycosyltransferase, is a target for proteasomal degradation. Mol. Biol. Cell 19:2169-2178. |
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Revision as of 06:09, 14 May 2008
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Systematic name | YGL047W |
Gene name | ALG13 |
Aliases | |
Feature type | ORF, Verified |
Coordinates | Chr VII:411555..412163 |
Primary SGDID | S000003015 |
Description of YGL047W: Catalytic component of UDP-GlcNAc transferase, required for the second step of dolichyl-linked oligosaccharide synthesis; anchored to the ER membrane via interaction with Alg14p; similar to bacterial and human glycosyltransferases[1][2][3]
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Contents
Community Commentary
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Cytosolic Alg13 not bound to Alg14 at the ER membrane is very short-lived.
Ubiquitin-independent proteasomal degradation is mediated by an autonomous C-terminal domain. Addition of C-terminal epitope tags interfere with Alg13 degradation Cite error: Closing </ref>
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References
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- ↑ Bickel T, et al. (2005) Biosynthesis of lipid-linked oligosaccharides in Saccharomyces cerevisiae: Alg13p and Alg14p form a complex required for the formation of GlcNAc(2)-PP-dolichol. J Biol Chem 280(41):34500-6 SGD PMID 16100113
- ↑ Gao XD, et al. (2005) Alg14 Recruits Alg13 to the Cytoplasmic Face of the Endoplasmic Reticulum to Form a Novel Bipartite UDP-N-acetylglucosamine Transferase Required for the Second Step of N-Linked Glycosylation. J Biol Chem 280(43):36254-62 SGD PMID 16100110
- ↑ Chantret I, et al. (2005) Two proteins homologous to the N- and C-terminal domains of the bacterial glycosyltransferase Murg are required for the second step of dolichyl-linked oligosaccharide synthesis in Saccharomyces cerevisiae. J Biol Chem 280(10):9236-42 SGD PMID 15615718
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