A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.

TitleA putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.
Publication TypeJournal Article
Year of Publication1990
AuthorsRothman JH, Raymond CK, Gilbert T, O'Hara PJ, Stevens TH
JournalCell
Volume61
Issue6
Pagination1063-74
Date Published1990 Jun 15
ISSN0092-8674
KeywordsAmino Acid Sequence, Animals, Antiviral Agents, Base Sequence, Carrier Proteins, Cloning, Molecular, Fluorescent Antibody Technique, Genotype, GTP-Binding Proteins, Immunoblotting, Molecular Sequence Data, Mutation, Myxovirus Resistance Proteins, Protein Biosynthesis, Protein Processing, Post-Translational, Proteins, Restriction Mapping, Saccharomyces cerevisiae, Sequence Homology, Nucleic Acid, Vertebrates, Vesicular Transport Proteins
Abstract

Members of the Mx protein family promote interferon-inducible resistance to viral infection in mammals and act by unknown mechanisms. We identified an Mx-like protein in yeast and present genetic evidence for its cellular function. This protein, the VPS1 product, is essential for vacuolar protein sorting, normal organization of intracellular membranes, and growth at high temperature, implying that Mx-like proteins are engaged in fundamental cellular processes in eukaryotes. Vps1p contains a tripartite GTP binding motif, which suggests that binding to GTP is essential to its role in protein sorting. Vps1p-specific antibody labels punctate cytoplasmic structures that condense to larger structures in a Golgi-accumulating sec7 mutant; thus, Vps1p may associate with an intermediate organelle of the secretory pathway.

Alternate JournalCell
PubMed ID2112425
Grant ListGM-32448 / GM / NIGMS NIH HHS / United States