کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1979181 | 1061665 | 2011 | 7 صفحه PDF | دانلود رایگان |

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.
► 10% of the human kinome contains lipid-binding domains.
► Kinases with novel lipid-binding domains are still being discovered.
► Recent kinase structures have provided new insights into their activation by lipids.
► A novel interface between the C1B and kinase domains controls PKCβII activation.
Journal: Current Opinion in Structural Biology - Volume 21, Issue 6, December 2011, Pages 785–791