Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors
0301 basic medicine
570
Protein Folding
Saccharomyces cerevisiae Proteins
Rhinovirus
Genetic Vectors
Green Fluorescent Proteins
Molecular Sequence Data
Autophagy-Related Proteins
612
Endosomes
Saccharomyces cerevisiae
12. Responsible consumption
03 medical and health sciences
Phosphatidylinositol Phosphates
Escherichia coli
Amino Acid Sequence
Cloning, Molecular
Base Sequence
Membrane Proteins
Phosphotransferases (Alcohol Group Acceptor)
Protein Transport
Gene Components
Plasmids
Protein Binding
DOI:
10.1038/sj.emboj.7600203
Publication Date:
2004-04-22T08:51:54Z
AUTHORS (12)
ABSTRACT
Phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2), made by Fab1p, is essential for vesicle recycling from vacuole/lysosomal compartments and for protein sorting into multivesicular bodies. To isolate PtdIns(3,5)P2 effectors, we identified Saccharomyces cerevisiae mutants that display fab1delta-like vacuole enlargement, one of which lacked the SVP1/YFR021w/ATG18 gene. Expressed Svp1p displays PtdIns(3,5)P2 binding of exquisite specificity, GFP-Svp1p localises to the vacuole membrane in a Fab1p-dependent manner, and svp1delta cells fail to recycle a marker protein from the vacuole to the Golgi. Cells lacking Svp1p accumulate abnormally large amounts of PtdIns(3,5)P2. These observations identify Svp1p as a PtdIns(3,5)P2 effector required for PtdIns(3,5)P2-dependent membrane recycling from the vacuole. Other Svp1p-related proteins, including human and Drosophila homologues, bind PtdIns(3,5)P2 similarly. Svp1p and related proteins almost certainly fold as beta-propellers, and the PtdIns(3,5)P2-binding site is on the beta-propeller. It is likely that many of the Svp1p-related proteins that are ubiquitous throughout the eukaryotes are PtdIns(3,5)P2 effectors. Svp1p is not involved in the contributions of FAB1/PtdIns(3,5)P2 to MVB sorting or to vacuole acidification and so additional PtdIns(3,5)P2 effectors must exist.
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