The Fab1 phosphatidylinositol kinase pathway in the regulation of vacuole morphology.
Yeast vacuoles are very dynamic structures that must respond to changes in extracellular osmolarity by rapidly altering their size, thereby releasing or taking up water and ions. Further, the need to accommodate a constant biosynthetic influx of membrane and to partition vacuoles during cell division necessitates precise regulation of the size and shape of the vacuole. While it is has been shown that the lipid kinase Fab1p and its product phosphatidylinositol 3,5-bisphosphate, and not the mitogen-activated protein kinase Hog1p, are central to this regulatory pathway, key effectors still await identification. Atg18p is the most recently identified candidate for a Fab1p effector mediating the largely uncharacterized processes of vesicle fission and membrane recycling at the vacuole.
Division of Biology, Department of Cellular and Molecular Medicine, and the Howard Hughes Medical Institute, University of California-San Diego, La Jolla, CA 92093-0668, USA.
Jem A
JA
Efe
Roberto J
RJ
Botelho
Scott D
SD
Emr
D007425:Intracellular Membranes / Q000378:metabolism; D017136:Ion Transport; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D009994:Osmolar Concentration; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D014617:Vacuoles / Q000378:metabolism*
D029701:Saccharomyces cerevisiae Proteins; C095504:FAB1 protein, S cerevisiae; D017853:Phosphotransferases (Alcohol Group Acceptor); C088589:HOG1 protein, S cerevisiae; D020928:Mitogen-Activated Protein Kinases