Cytoplasmic peptide:N-glycanase cleaves N-glycans on a carboxypeptidase Y mutant during ERAD in Saccharomyces cerevisiae.
In: BBA - General Subjects, Jg. 1850 (2015-04-01), Heft 4, S. 612-619
academicJournal
Zugriff:
Background Endoplasmic reticulum (ER)-associated degradation (ERAD) is a pathway by which misfolded or improperly assembled proteins in the ER are directed to degradation. The cytoplasmic peptide: N -glycanase (PNGase) is a deglycosylating enzyme that cleaves N -glycans from misfolded glycoproteins during the ERAD process. The mutant form of yeast carboxypeptidase Y (CPY*) is an ERAD model substrate that has been extensively studied in yeast. While a delay in the degradation of CPY* in yeast cells lacking the cytoplasmic PNGase (Png1 in yeast) was evident, the in vivo action of PNGase on CPY* has not been detected. Methods We constructed new ERAD substrates derived from CPY*, bearing epitope tags at both N- and C-termini and examined the degradation intermediates observed in yeast cells with compromised proteasome activity. Results The occurrence of the PNGase-mediated deglycosylation of intact CPY* and its degradation intermediates was evident. A major endoproteolytic reaction on CPY* appears to occur between amino acid 400 and 404. Conclusions The findings reported herein clearly indicate that PNGase indeed releases N -glycans from CPY* during the ERAD process in vivo . General Significance This report implies that the PNGase-mediated deglycosylation during the ERAD process may occur more abundantly than currently envisaged. [ABSTRACT FROM AUTHOR]
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Cytoplasmic peptide:N-glycanase cleaves N-glycans on a carboxypeptidase Y mutant during ERAD in Saccharomyces cerevisiae.
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Autor/in / Beteiligte Person: | Hosomi, Akira ; Suzuki, Tadashi |
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Zeitschrift: | BBA - General Subjects, Jg. 1850 (2015-04-01), Heft 4, S. 612-619 |
Veröffentlichung: | 2015 |
Medientyp: | academicJournal |
ISSN: | 0304-4165 (print) |
DOI: | 10.1016/j.bbagen.2014.12.008 |
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