Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Academic Article uri icon

Overview

abstract

  • Sorting of signal-transducing cell surface receptors within multivesicular bodies (MVBs) is required for their rapid down-regulation and degradation within lysosomes. Yeast mutants defective in late stages of transport to the vacuole/lysosome accumulate MVBs. We demonstrate that the membrane glycoprotein carboxypeptidase S and the G protein-coupled receptor Ste2p are targeted into the vacuole lumen, and this process requires a subset of VPS gene products essential for normal endosome function. The PtdIns(3)P 5-kinase activity of Fab1p, which converts the product of the Vps34p PtdIns 3-kinase PtdIns(3)P into PtdIns(3,5)P2, also is required for cargo-selective sorting into the vacuole lumen. These findings demonstrate a role for phosphoinositide signaling at distinct stages of vacuolar/lysosomal protein transport and couple PtdIns(3,5)P2 synthesis to regulation of MVB sorting.

publication date

  • December 11, 1998

Research

keywords

  • Adenosine Triphosphatases
  • Carboxypeptidases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Saccharomyces cerevisiae Proteins

Identity

Scopus Document Identifier

  • 0032217266

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)81707-9

PubMed ID

  • 9865702

Additional Document Info

volume

  • 95

issue

  • 6