Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae

• Published in: Journal of cell science Vol. 116; no. Pt 19; pp. 3957 - 3970
• Main Authors: Yeo, Sebastian C L, Xu, Linghui, Ren, Jihui, Boulton, Victoria J, Wagle, Mahendra D, Liu, Cong, Ren, Gang, Wong, Peisze, Zahn, Regina, Sasajala, Piriya, Yang, Hongyuan, Piper, Robert C, Munn, Alan L
• Format: Journal Article
• Language: English
• Published: England 01.10.2003
• Subjects: Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Biological Transport - physiology; Carboxypeptidases - metabolism; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cathepsin A; Cloning, Molecular; Endosomal Sorting Complexes Required for Transport; Endosomes - metabolism; Membrane Proteins - genetics; Membrane Proteins - metabolism; Mutation; Protein Binding; Protein Structure, Tertiary; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Transport Vesicles - metabolism; Two-Hybrid System Techniques; Vesicular Transport Proteins

Vps4p (End13p) is an AAA-family ATPase that functions in membrane transport through endosomes, sorting of soluble vacuolar proteins to the vacuole, and multivesicular body (MVB) sorting of membrane proteins to the vacuole lumen. In a yeast two-hybrid screen with Vps4p as bait we isolated VPS20 (YMR0...