[Novel deglycosylation-independent roles for peptide N-glycanase].
The primary function of peptide N-glycanase (PNGase) is thought to be the deglycosylation of endoplasmic reticulum associated degradation (ERAD) substrates. However, inhibition of PNGase appears to have little effect upon the destruction rate of many ERAD substrates, and recent data demonstrate deglycosylation-independent functions for PNGase. Whatever the roles of PNGase turn out to be, the identification of a patient presenting with PNGase deficiency will advance our understanding of the importance of this multifunctional protein in human physiology.
Inserm U773, centre de recherche Bichat Beaujon CRB3, Faculté de médecine Xavier Bichat, 75018 Paris, France - Université Paris 7 Denis Diderot, site Bichat, 16, rue Henri Huchard, 75018, Paris, France.
Isabelle
I
Chantret
Inserm U773, centre de recherche Bichat Beaujon CRB3, Faculté de médecine Xavier Bichat, 75018 Paris, France - Université Paris 7 Denis Diderot, site Bichat, 16, rue Henri Huchard, 75018, Paris, France.
Alain
A
Couvineau
Inserm U773, centre de recherche Bichat Beaujon CRB3, Faculté de médecine Xavier Bichat, 75018 Paris, France - Université Paris 7 Denis Diderot, site Bichat, 16, rue Henri Huchard, 75018, Paris, France.
Stuart
S
Moore
D000595:Amino Acid Sequence; D000818:Animals; D015870:Gene Expression; D006031:Glycosylation; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / Q000737:chemistry / Q000502:physiology*; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase