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Physiol. Rev. 84: 699-730, 2004; doi:10.1152/physrev.00033.2003
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Phosphoinositides in Constitutive Membrane Traffic

Michael G. Roth

Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas

Proteins that make, consume, and bind to phosphoinositides are important for constitutive membrane traffic. Different phosphoinositides are concentrated in different parts of the central vacuolar pathway, with phosphatidylinositol 4-phosphate predominate on Golgi, phosphatidylinositol 4,5-bisphosphate predominate at the plasma membrane, phosphatidylinositol 3-phosphate the major phosphoinositide on early endosomes, and phosphatidylinositol 3,5-bisphosphate found on late endocytic organelles. This spatial segregation may be the mechanism by which the direction of membrane traffic is controlled. Phosphoinositides increase the affinity of membranes for peripheral membrane proteins that function for sorting protein cargo or for the docking and fusion of transport vesicles. This implies that constitutive membrane traffic may be regulated by the mechanisms that control the activity of the enzymes that produce and consume phosphoinositides. Although the lipid kinases and phosphatases that function in constitutive membrane traffic are beginning to be identified, their regulation is poorly understood.

1 In this review phosphatidylinositol is abbreviated PtdIns. The phosphorylated phosphatidylinositols are referred to as phosphoinositides, abbreviated as PIPs. Kinases that can act on either PtdIns or PIP are abbreviated as PIXK, where X refers to the position on the inositol head group that is modified. Kinases that act only on PIPs and not PtdIns are referred to as PIPXK. Kinases that only phosphorylate PtdIns are abbreviated as PtdInsXK.

Address for reprint requests and other correspondence: M. G. Roth, Dept. of Biochemistry, Univ. of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd., Dallas, TX 75390-9038 (E-mail: michael.roth{at}utsouthwestern.edu).




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