An Integral Membrane Component of Coatomer-Coated Transport Vesicles Defines a Family of Proteins Involved in Budding

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 17; pp. 8011 - 8015
• Main Authors: Stamnes, Mark A., Craighead, Mark W., Hoe, Mee H., Lampen, Nina, Geromanos, Scott, Tempst, Paul, Rothman, James E.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 15.08.1995; National Acad Sciences
• Subjects: ADP-Ribosylation Factors; Amino Acid Sequence; Animals; Arabidopsis - metabolism; Base Sequence; Brain - metabolism; Budding; Carrier Proteins - metabolism; Cattle; CHO Cells; Coated vesicles; Coatomer Protein; COP coated vesicles; Cricetinae; Cytosol; Cytosol - metabolism; DNA Primers; Dogs; Family members; Golgi Apparatus - metabolism; Golgi Apparatus - ultrastructure; GTP-Binding Proteins - metabolism; Humans; Membrane Fusion; Membrane proteins; Membrane Proteins - biosynthesis; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Microscopy, Electron; Molecular Sequence Data; Organelles - physiology; P branes; Polymerase Chain Reaction; Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae - physiology; Sequence Homology, Amino Acid; Yeasts
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.92.17.8011

We have isolated a major integral membrane protein from Golgi-derived coatomer-coated vesicles. This 24-kDa protein, p24, defines a family of integral membrane proteins with homologs present in yeast and humans. In addition to sequence similarity, all p24 family members contain a motif with the characteristic heptad repeats found in coiled coils. When the yeast p24 isoform, yp24A, is knocked out in a strain defective for vesicle fusion, a dramatic reduction in the accumulation of transport vesicles is observed. Together, these results indicate a role for this protein family in the budding of coatamer-coated and other species of coated vesicles.