Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Annu Rev Biophys Biomol Struct. 2002;31:151-75. Epub 2001 Oct 25.

PIP(2) and proteins: interactions, organization, and information flow.

Author information

  • 1Department of Physiology and Biophysics, HSC, SUNY Stony Brook, NY 11794-8661, USA. SMCL@epo.som.sunysb.edu

Abstract

We review the physical properties of phosphatidylinositol 4,5-bisphosphate (PIP2) that determine both its specific interactions with protein domains of known structure and its nonspecific electrostatic sequestration by unstructured domains. Several investigators have postulated the existence of distinct pools of PIP2 within the cell to account for the myriad functions of this lipid. Recent experimental work indicates certain regions of the plasma membrane-membrane ruffles and nascent phagosomes-do indeed concentrate PIP2. We consider two mechanisms that could account for this phenomenon: local synthesis and electrostatic sequestration. We conclude by considering the hypothesis that proteins such as MARCKS bind a significant fraction of the PIP2 in a cell, helping to sequester it in lateral membrane domains, then release this lipid in response to local signals such as an increased concentration of Ca(++)/calmodulin or activation of protein kinase C.

PMID:
11988466
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Atypon
    Loading ...
    Write to the Help Desk