Regulation of protein kinases by lipids.

Abstract:

:Membranes are sites of intense signaling activity within the cell, serving as dynamic scaffolds for the recruitment of signaling molecules and their substrates. The specific and reversible localization of these signaling molecules to membranes is critical for the appropriate activation of downstream signaling pathways. Phospholipid-binding domains, including C1, C2, PH, and PX domains, play critical roles in the membrane targeting of protein kinases. Recent structural studies have identified a new membrane association domain, the Kinase Associated 1 (KA1) domain, which targets a number of yeast and mammalian protein kinases to membranes containing acidic phospholipids. Despite an abundance of localization studies on lipid-binding proteins and structural studies of the isolated lipid-binding domains, the question of how membrane binding is coupled to the activation of the kinase catalytic domain has been virtually untouched. Recently, structural studies on protein kinase C (PKC) have provided some of the first structural insights into the allosteric regulation of protein kinases by lipid second messengers.

journal_name

Curr Opin Struct Biol

authors

Leonard TA,Hurley JH

doi

10.1016/j.sbi.2011.07.006

subject

Has Abstract

pub_date

2011-12-01 00:00:00

pages

785-91

issue

6

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(11)00129-1

journal_volume

21

pub_type

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