spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
JCS ePress online publication date 15 Mar 2005
doi: 10.1242/jcs.01740

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.01740v1
118/7/1485    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kostova, Z.
Right arrow Articles by Wolf, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kostova, Z.
Right arrow Articles by Wolf, D. H.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Research Article

Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation


Zlatka Kostova and Dieter H. Wolf*
* Author for correspondence (e-mail: dieter.wolf{at}ibc.uni-stuttgart.de)

In the endoplasmic reticulum (ER), N-linked glycans (N-glycans) function as signals to recruit the lectin chaperones involved in protein folding, quality control and ER-associated degradation. We undertook a systematic study of the four N-glycans of mutated carboxypeptidase yscY (CPY*) to determine whether there are positional differences between the glycans in ER-associated degradation. We constructed hypoglycosylated CPY* variants containing one, two or three N-glycans in various combinations and studied their degradation kinetics. We found that the four carbohydrate chains on CPY* are not equal in their signaling function: presence of the Asn368-linked glycan is necessary and sufficient for efficient degradation of CPY*. We also analysed the involvement of the ER lectins Htm1p and Cne1p (yeast calnexin) in the glycan-based recognition process with respect to number and position of N-glycans. We observed that Htm1p function depends on the presence of N-glycans in general but that there is no positional preference for a particular glycan. Cne1p, however, is selective with respect to substrate, and participates in the quality control only of some underglycosylated variants. For cases in which both lectins are involved, Cne1p and Htm1p play competing roles in targeting the substrate for degradation: loss of Cne1p accelerates degradation, whereas loss of Htm1p stabilizes the substrate.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
W. Xie, K. Kanehara, A. Sayeed, and D. T.W. Ng
Intrinsic Conformational Determinants Signal Protein Misfolding to the Hrd1/Htm1 Endoplasmic Reticulum-associated Degradation System
Mol. Biol. Cell, July 15, 2009; 20(14): 3317 - 3329.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
Z. Kostova, J. Mariano, S. Scholz, C. Koenig, and A. M. Weissman
A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation
J. Cell Sci., May 1, 2009; 122(9): 1374 - 1381.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
S. Clerc, C. Hirsch, D. M. Oggier, P. Deprez, C. Jakob, T. Sommer, and M. Aebi
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
J. Cell Biol., January 12, 2009; 184(1): 159 - 172.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
X.-b. Chang, A. Mengos, Y.-x. Hou, L. Cui, T. J. Jensen, A. Aleksandrov, J. R. Riordan, and M. Gentzsch
Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator
J. Cell Sci., September 1, 2008; 121(17): 2814 - 2823.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
H. Hirayama, M. Fujita, T. Yoko-o, and Y. Jigami
O-Mannosylation is Required for Degradation of the Endoplasmic Reticulum-associated Degradation Substrate Gas1*p via the Ubiquitin/Proteasome Pathway in Saccharomyces cerevisiae
J. Biochem., April 1, 2008; 143(4): 555 - 567.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Kario, B. Tirosh, H. L. Ploegh, and A. Navon
N-Linked Glycosylation Does Not Impair Proteasomal Degradation but Affects Class I Major Histocompatibility Complex Presentation
J. Biol. Chem., January 4, 2008; 283(1): 244 - 254.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
I. Shapira, D. Charuvi, Y. Elkabetz, K. Hirschberg, and S. Bar-Nun
Distinguishing between retention signals and degrons acting in ERAD
J. Cell Sci., December 15, 2007; 120(24): 4377 - 4387.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
S.-H. Park, N. Bolender, F. Eisele, Z. Kostova, J. Takeuchi, P. Coffino, and D. H. Wolf
The Cytoplasmic Hsp70 Chaperone Machinery Subjects Misfolded and Endoplasmic Reticulum Import-incompetent Proteins to Degradation via the Ubiquitin-Proteasome System
Mol. Biol. Cell, January 1, 2007; 18(1): 153 - 165.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2005