Par‐6 activates atypical Protein Kinase C by pseudosubstrate displacement
نویسندگان
چکیده
منابع مشابه
Caspase processing activates atypical protein kinase C zeta by relieving autoinhibition and destabilizes the protein.
Treatment of HeLa cells with tumour necrosis factor alpha (TNFalpha) induced caspase processing of ectopic PKC (protein kinase C) zeta, which converted most of the holoenzyme into the freed kinase domain and increased immune-complex kinase activity. The goal of the present study was to determine the basis for the increased kinase activity that is associated with caspase processing of PKC zeta. ...
متن کاملPB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62.
Maximal activation of NADPH oxidase requires formation of a complex between the p40(phox) and p67(phox) subunits via association of their PB1 domains. We have determined the crystal structure of the p40(phox)/p67(phox) PB1 heterodimer, which reveals that both domains have a beta grasp topology and that they bind in a front-to-back arrangement through conserved electrostatic interactions between...
متن کاملComplete activation of protein kinase C by an antipeptide antibody directed against the pseudosubstrate prototope.
It has been proposed that the regulatory domain of protein kinase C contains a pseudosubstrate site between amino acid residues 19 and 36 (House, C., and Kemp, B. E. (1987) Science 238, 1726-1728). Antiserum raised against this peptide sequence has now been shown to completely activate protein kinase C in the absence of calcium and phospholipids. Pre-clearing the antiserum with resin-immobilize...
متن کاملDual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol.
The activity of protein kinase C is reversibly regulated by an autoinhibitory pseudosubstrate, which blocks the active site of the enzyme in the absence of activators. However, before it can be allosterically regulated, protein kinase C must first be processed by three ordered phosphorylations, the first of which is modification of the activation loop catalyzed by the phosphoinositide-dependent...
متن کاملAtypical protein kinase C (iota) activates ezrin in the apical domain of intestinal epithelial cells.
Atypical protein kinase iota (PKCiota) is a key organizer of the apical domain in epithelial cells. Ezrin is a cytosolic protein that, upon activation by phosphorylation of T567, is localized under the apical membrane where it connects actin filaments to membrane proteins and recruits protein kinase A (PKA). To identify the kinase that phosphorylates ezrin T567 in simple epithelia, we analyzed ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2012
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.26.1_supplement.756.18