Format

Send to:

Choose Destination
See comment in PubMed Commons below
Crit Rev Biochem Mol Biol. 2007 Jan-Feb;42(1):15-39.

A conspicuous connection: structure defines function for the phosphatidylinositol-phosphate kinase family.

Author information

  • 1Program in Molecular and Cellular Pharmacology, Department of Pharmacology, University of Wisconsin-Madison, University of Wisconsin Medical School, Madison, WI 53706, USA.

Erratum in

  • Crit Rev Biochem Mol Biol. 2007 May-Jun;42(3):243.

Abstract

The phosphatidylinositol phosphate (PIP) kinases are a unique family of enzymes that generate an assortment of lipid messengers, including the pivotal second messenger phosphatidylinositol 4,5-bisphosphate (PI4,5P2). While members of the PIP kinase family function by catalyzing a similar phosphorylation reaction, the specificity loop of each PIP kinase subfamily determines substrate preference and partially influences distinct subcellular targeting. Specific protein-protein interactions that are unique to particular isoforms or splice variants play a key role in targeting PIP kinases to appropriate subcellular compartments to facilitate the localized generation of PI4,5P2 proximal to effectors, a mechanism key for the function of PI4,5P2 as a second messenger. This review documents the discovery of the PIP kinases and their signaling products, and summarizes our current understanding of the mechanisms underlying the localized generation of PI4,5P2 by PIP kinases for the regulation of cellular events including actin cytoskeleton dynamics, vesicular trafficking, cell migration, and an assortment of nuclear events.

PMID:
17364683
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Taylor & Francis
    Loading ...
    Write to the Help Desk