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Semin Cell Dev Biol. 2007 Dec;18(6):762-9. Epub 2007 Sep 16.

Cytoplasmic peptide:N-glycanase and catabolic pathway for free N-glycans in the cytosol.

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1
Department of Biochemistry, 21st Center of Excellence Program, Osaka University Graduate School of Medicine, Japan. tsuzuki_gm@riken.jp

Abstract

Peptide:N-glycanase (PNGase) releases N-glycans from glycoproteins/glycopeptides. Cytoplasmic PNGase is widely recognized as a component of machinery for ER-associated degradation (ERAD), i.e. proteasomal degradation of misfolded, newly synthesized (glyco)proteins that have been exported from the ER. The enzyme belongs to the "transglutaminase superfamily" that contains a putative catalytic triad of cysteine, histidine, and aspartic acid. The mammalian orthologues of PNGase contain the N-terminal PUB domain that serves as the protein-protein interaction domain. The C-terminus of PNGase was recently found to be a novel carbohydrate-binding domain. Taken together, these observations indicate that C-terminus of mammalian PNGase is important for recognition of the substrates while N-terminus of this enzyme is involved in assembly of a degradation complex.

PMID:
17950635
DOI:
10.1016/j.semcdb.2007.09.010
[Indexed for MEDLINE]
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