Glycoprotein Processing Systems of Er and Golgi

Robbins, Phillips W.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM045188-06
• Application #: 2182977
• Study Section: Pathobiochemistry Study Section (PBC)
• Project Start: 1991-01-01
• Project End: 1998-12-31
• Budget Start: 1996-01-01
• Budget End: 1996-12-31
• Support Year: 6
• Fiscal Year: 1996

Institution

• Name: Massachusetts Institute of Technology
• Type: Organized Research Units
• City: Cambridge
• State: MA
• Country: United States
• Zip Code: 02139

Publications

Zimmerman, J W; Robbins, P W (1993) The hydrophobic domain of dolichyl-phosphate-mannose synthase is not essential for enzyme activity or growth in Saccharomyces cerevisiae. J Biol Chem 268:16746-53

Schutzbach, J S; Zimmerman, J W; Forsee, W T (1993) The purification and characterization of recombinant yeast dolichyl-phosphate-mannose synthase. Site-directed mutagenesis of the putative dolichol recognition sequence. J Biol Chem 268:24190-6

Abeijon, C; Yanagisawa, K; Mandon, E C et al. (1993) Guanosine diphosphatase is required for protein and sphingolipid glycosylation in the Golgi lumen of Saccharomyces cerevisiae. J Cell Biol 122:307-23

Hausler, A; Robbins, P W (1992) Glycosylation in Saccharomyces cerevisiae: cloning and characterization of an alpha-1,2-mannosyltransferase structural gene. Glycobiology 2:77-84

Schutzbach, J S; Zimmerman, J W (1992) Yeast dolichyl-phosphomannose synthase: reconstitution of enzyme activity with phospholipids. Biochem Cell Biol 70:460-5

Hausler, A; Ballou, L; Ballou, C E et al. (1992) Yeast glycoprotein biosynthesis: MNT1 encodes an alpha-1,2-mannosyltransferase involved in O-glycosylation. Proc Natl Acad Sci U S A 89:6846-50