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Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbalip.2007.01.015

Keywords

phosphoinositide; phosphatidylinositol kinases; phosphoinositide phosphatases; secretory pathway; vesicle-mediated protein transport; exocytosis; endocytosis; vacuolar protein sorting; autophagy; plasma membrane; golgi membrane; nucleus

Funding

  1. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM021841, R37GM021841] Funding Source: NIH RePORTER
  2. NIGMS NIH HHS [R01 GM021841, GM21841] Funding Source: Medline

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It is now well appreciated that derivatives of phosphatidylinositol (PtdIns) are key regulators of many cellular processes in eukaryotes. Of particular interest are phosphoinositides (mono- and polyphosphorylated adducts to the inositol ring in PtdIns), which are located at the cytoplasmic face of cellular membranes. Phosphoinositides serve both a structural and a signaling role via their recruitment of proteins that contain phosphoinositide-binding domains. Phosphoinositides also have a role as precursors of several types of second messengers for certain intracellular signaling pathways. Realization of the importance of phosphoinositides has brought increased attention to characterization of the enzymes that regulate their synthesis, interconversion, and turnover. Here we review the current state of our knowledge about the properties and regulation of the ATP-dependent lipid kinases responsible for synthesis of phosphoinositides and also the additional temporal and spatial controls exerted by the phosphatases and a phospholipase that act on phosphoinositides in yeast. (c) 2007 Elsevier B.V. All rights reserved.

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