XB-ART-55962
Biochem Biophys Res Commun
2018 Nov 25;5062:307-314. doi: 10.1016/j.bbrc.2018.07.155.
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Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms.
Janmey PA
,
Bucki R
,
Radhakrishnan R
.
Abstract
Actin cytoskeleton dynamics depend on a tight regulation of actin filament formation from an intracellular pool of monomers, followed by their linkage to each other or to cell membranes, followed by their depolymerization into a fresh pool of actin monomers. The ubiquitous requirement for continuous actin remodeling that is necessary for many cellular functions is orchestrated in large part by actin binding proteins whose affinity for actin is altered by inositol phospholipids, most prominently PI(4,5)P2 (phosphatidylinositol 4,5-bisphosphate). The kinetics of PI(4,5)P2 synthesis and hydrolysis, its lateral distribution within the lipid bilayer, and coincident detection of PI(4,5)P2 and another signal, all play a role in determining when and where a particular PI(4,5)P2-regulated protein is inactivated or activated to exert its effect on the actin cytoskeleton. This review summarizes a range of models that have been developed to explain how PI(4,5)P2 might function in the complex chemical and structural environment of the cell based on a combination of experiment and computational studies.
PubMed ID: 30139519
PMC ID: PMC6269227
Article link: Biochem Biophys Res Commun
Grant support: [+]
Species referenced: Xenopus laevis
Genes referenced: actn1 actn2 actn3 actn4 ezr flna fmn1 fmn2 fmnl1 fmnl2 fmnl3 gsn tln1 vcl was
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