We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
PIP(2) and proteins: interactions, organization, and information flow.
- Authors
McLaughlin, Stuart; Wang, Jiyao; Gambhir, Alok; Murray, Diana
- 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.
- Publication
Annual review of biophysics and biomolecular structure, 2002, Vol 31, p151
- ISSN
1056-8700
- Publication type
Journal Article
- DOI
10.1146/annurev.biophys.31.082901.134259