Rad23 Provides a Link between the Png1 Deglycosylating Enzyme and the 26 S Proteasome in Yeast

Suzuki, Tadashi; Park, Hangil; Kwofie, Michael A.; Lennarz, William J.

doi:10.1074/jbc.m100826200

Cited by 111 publications

(114 citation statements)

References 55 publications

(46 reference statements)

Supporting

Mentioning

105

Contrasting

Unclassified

Order By: Relevance

“…2A, top, blue trace). Although amyloglucosidase cleaves ␣1,3-, ␣1,4-, and ␣1,6-glucose residues, it is possible that peaks a-e do not correspond to oligomers of ␣-linked glucose but rather correspond to ␤-glucans previously described to occur in yeast (Glc [3][4][5][6][7][8][9][10][11][12][13][14][15] (21)) because the amyloglucosidase preparation used in our studies is probably contaminated with ␤-glucanase (31). Another oligosaccharide pool was noted in both wild type and ams1⌬ cells but occurred in strikingly 3 I. Chantret and S. E. H. Moore, unpublished data.…”

Section: Png1p-dependent Fos Are Regulated During Post-diauxic Growthmentioning

confidence: 98%

Endoplasmic Reticulum-associated Degradation (ERAD) and Free Oligosaccharide Generation in Saccharomyces cerevisiae

Chantret

Kodali

Lahmouich

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Yeast free oligosaccharides (fOS) are cleaved from glycoproteins during ER-associated degradation of proteins (ERAD), but factors underlying their control remain to be explored. Results: Only one-half of fOS are regulated by known ERAD processes, and fOS generation and demannosylation are growth-dependent. Conclusion: Additional complexity of ERAD processes is revealed. Significance: This is the first demonstration of growth-dependent fOS regulation.

show abstract

Section: Png1p-dependent Fos Are Regulated During Post-diauxic Growthmentioning

confidence: 98%

Endoplasmic Reticulum-associated Degradation (ERAD) and Free Oligosaccharide Generation in Saccharomyces cerevisiae

Chantret

Kodali

Lahmouich

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…PNGase is highly conserved in eukaryotes and possesses a catalytic Cys, His, and Asp triad embedded in a transglutaminase fold. Both mouse and yeast PNGase have been reported to interact with HR23B͞Rad23, a protein that is also involved in DNA damage recognition (5)(6)(7). Recently the structures of yeast and mouse PNGase in complex with Rad23͞ HR23B and an inhibitor (8), carbobenzyloxy-Val-Ala-Asp-␣-fluoromethyl ketone (Z-VAD-fmk), have been solved (9,10).…”

mentioning

confidence: 99%

Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module

Zhou

Zhao

Truglio

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

The inability of certain N-linked glycoproteins to adopt their native conformation in the endoplasmic reticulum (ER) leads to their retrotranslocation into the cytosol and subsequent degradation by the proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is highly conserved in eukaryotes and plays an important role in ER-associated protein degradation. In higher eukaryotes, PNGase has an N-terminal and a C-terminal extension in addition to its central catalytic domain, which is structurally and functionally related to transglutaminases. Although the N-terminal domain of PNGase is involved in protein-protein interactions, the function of the C-terminal domain has not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal domain, including visualization of a complex between this domain and mannopentaose. These studies demonstrate that the C-terminal domain binds to the mannose moieties of N-linked oligosaccharide chains, and we further show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins.endoplasmic reticulum ͉ N-linked glycoproteins ͉ proteasome ͉ protein degradation ͉ deglycosylation

show abstract

“…A yeast two-hybrid screen and biochemical studies detected the interaction of cytoplasmic yeast PNGase (yPNGase) with yRpt1 (a 19S proteasome subunit) through yRad23 (a yeast nucleotide excision repair protein), and this complex has been implicated in the ERAD pathway (7). yRpt1 interacts with yRpt2 (8,9), a protein that has been shown to mediate gating of the proteasome by means of its ATPase domain (10).…”

mentioning

confidence: 99%

A complex between peptide: N -glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins

Katiyar

Lennarz

2004

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Peptide:N-glycanase (PNGase) has been proposed to participate in the proteasome-dependent glycoprotein degradation pathway. The finding that yeast PNGase interacts with the 19S proteasome subunit through the protein Rad23 supports this hypothesis. In this report, we have used immunofluorescence, subcellular fractionation, coimmunoprecipitation, and in vitro GST pull-down techniques for detecting intracellular localization and interactions of PNGase, HR23B, and S4 by using human (h) and mouse (m) homologs. Immunofluorescence studies revealed that hPNGase, hHR23B, and hS4 are present in close proximity to the endoplasmic reticulum (ER) when calnexin was used as an ER marker in HeLa cells. Subcellular fractionation suggests not only cytoplasmic but also ER association of hPNGase in HeLa cells. Immunoprecipitation analysis revealed the interaction of h͞mPNGase with the 19S proteasome subunit, hS4, through hHR23B. Using an in vitro GST pull-down assay, we also have shown that recombinant mPNGase requires its N terminus and middle domain for interaction with mHR23B. Finally, using misfolded yeast carboxypeptidase Y and chicken ovalbumin as glycoprotein substrates, we have established that mHR23B acts as a receptor for deglycosylated proteins. Based on this finding, we propose that after deglycosylation of misfolded glycoproteins by PNGase, the aglyco forms of these proteins are recognized by HR23B and targeted for degradation.

show abstract

Rad23 Provides a Link between the Png1 Deglycosylating Enzyme and the 26 S Proteasome in Yeast

Cited by 111 publications

References 55 publications

Endoplasmic Reticulum-associated Degradation (ERAD) and Free Oligosaccharide Generation in Saccharomyces cerevisiae

Endoplasmic Reticulum-associated Degradation (ERAD) and Free Oligosaccharide Generation in Saccharomyces cerevisiae

Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module

A complex between peptide: N -glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins

Contact Info

Product

Resources

About