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Fig. 3. (A) A model for the role of Vam7p in vesicle-vacuole docking. Vam7p is localised to the vacuole by interaction of its PX domain with PtdIns(3)P and through interaction with Vam3 (explaining how overexpression of Vam7p{Delta}PX can still facilitate docking, as it can be localised through Vam3, albeit to a lower extent than the wild type). The cargo vesicle docks to Vam7p through Vti1, and the Class C Vps complex also joins. Assembly of this complex facilitates vesicle-vacuole fusion (Sato et al., 2000). (B) A model of regulation of CISK by interaction with phosphoinositides. CISK is localised to membranes by PtdIns(3)P or PtdIns(3,4,5)P3. This may allow it to be activated through phosphorylation by an upstream kinase, perhaps PDK or a PDK-like kinase. Once active, CISK can phosphorylate downstream targets to exert effects on cell survival.





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