Abrogation of glucosidase I–mediated glycoprotein deglucosylation results in a sick phenotype in fission yeasts: Model for the human MOGS-CDG disorder

Glucosidase I (GI) removes the outermost glucose from protein-linked Glc 3 Man 9 GlcNAc 2 (G3M9) in the endoplasmic reticulum (ER). Individuals with congenital disorders of glycosylation MOGS-CDG bear mutations in the GI-encoding gene (gls1). Although GI absence has been reported to produce lethalit...

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Detalles Bibliográficos
Autores principales: Gallo, G.L., Valko, A., Aramburu, S.I., Etchegaray, E., Völker, C., Parodi, A.J., D’Alessio, C.
Formato: JOUR
Materias:
glucosidase
glucosidase I
glucosyltransferase
unclassified drug
Article
bioaccumulation
cell death
cell elongation
cellular distribution
chemical modification
conformation
congenital disorder of glycosylation
controlled study
deglucosylation
endoplasmic reticulum
enzyme activity
fungal cell
fungal cell wall
fungus growth
gene mutation
nonhuman
phenotype
priority journal
protein degradation
protein expression
protein folding
protein misfolding
Schizosaccharomyces pombe
transmission electron microscopy
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219258_v293_n52_p19957_Gallo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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