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A more recent version of this article appeared on February 1, 2002
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Submitted on October 1, 2001
Revised on November 14, 2001
Accepted on November 19, 2001
1 Division of Cellular and Molecular Medicine, The Howard Hughes Medical Institute, University of California, San Diego, School of Medicine, La Jolla, CA 92093-0068
* Corresponding author. E-mail address: semr{at}ucsd.edu.
Phosphoinositides (PI) are synthesized and turned over by specific kinases, phosphatases, and lipases that ensure the proper localization of discrete PI isoforms at distinct membranes. We analyzed the role of the yeast synaptojanin-like proteins using a strain that expressed only a temperature-conditional allele of SJL2. Our analysis demonstrated that inactivation of the yeast synaptojanins leads to increased cellular levels of PtdIns(3,5)P2 and PtdIns(4,5)P2, accompanied by defects in actin organization, endocytosis, and clathrin-mediated sorting between the Golgi and endosomes. The phenotypes observed in synaptojanin-deficient cells correlated with accumulation of PtdIns(4,5)P2, as these effects were rescued by mutations in MSS4 or a mutant form of Sjl2p that only harbors PI 5-phosphatase activity. We utilized GFP-PH chimeras (termed FLAREs for fluorescent lipid-associated reporters) with distinct PI-binding specificities to visualize pools of PtdIns(4,5)P2 and PtdIns(4)P in yeast. PtdIns(4,5)P2 localized to the plasma membrane in a manner dependent on Mss4p activity. Upon inactivation of the yeast synaptojanins, PtdIns(4,5)P2 accumulated on intracellular compartments, as well as the cell surface. In contrast, PtdIns(4)P generated by Pik1p localized on intracellular compartments. Taken together, our results demonstrate that the yeast synaptojanins control the localization of PtdIns(4,5)P2 in vivo and provide further evidence for the compartmentalization of different PI species.
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