NDLI: Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome

Content Provider	PubMed Central
Author	Li, Guangtao Zhou, Xiaoke Zhao, Gang Hermann, Schindelin Lennarz, William J.
Copyright Year	2005
Abstract	Peptide N-glycanase (PNGase) is involved in the cleavage of oligosaccharide chains from misfolded glycoproteins that are destined for degradation by the proteasome. Earlier, a number of potential binding partners of mouse PNGase (mPNGase) were detected by using the yeast two-hybrid system. In the current study, an in vitro system was set up to investigate direct interactions between mPNGase and these candidate proteins. Although the yeast two-hybrid system suggested an interaction of six different proteins with mPNGase, only mHR23B and the proteasome subunit mS4 were found to interact with mPNGase. In fact, mS4 competes with mHR23B for binding to mPNGase. These results suggested two possible pathways for the interaction between mPNGase and the proteasome. In one pathway, mHR23B mediates the interaction between mPNGase and the proteasome. In an alternative pathway, mPNGase directly binds to the proteasome subunit, mS4. In either case, it is clear that PNGase is located in close proximity to the proteasome and is available for deglycosylation of glycoproteins destined for degradation. Surprisingly, mPNGase also was found to mediate binding of the cytoplasmic protein, p97, to the proteasome through the formation of a ternary complex made up of mHR23B, mPNGase, and p97. Because p97 is known to bind to the endoplasmic reticulum membrane protein AMFR (gp78), an E3 ligase, we propose a model in which p97, mPNGase, and mHR23B mediate interaction of the endoplasmic reticulum with the proteasome.
Related Links	http://dx.doi.org/10.1073/pnas.0507155102
Ending Page	15814
Page Count	6
Starting Page	15809
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	44
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-11-01
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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