scholarly journals Down regulation of protein kinase C in neuronal cells: effects on neurotransmitter release

1987 ◽  
Vol 7 (4) ◽  
pp. 1198-1206 ◽  
Author(s):  
HJ Matthies ◽  
HC Palfrey ◽  
LD Hirning ◽  
RJ Miller
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Neurotransmitter Release ◽  
Neuronal Cells ◽  
Down Regulation ◽  
Kinase C

Possible involvement of protein kinase C activation in down-regulation of CD3 antigen on adult T cell leukaemia cells

1994 ◽  
Vol 86 (2) ◽  
pp. 399-401 ◽  
Author(s):  
Mitsuhiro Matsuda ◽  
Yasuhiro Maeda ◽  
Chikashi Shirakawa ◽  
Satoshi Morita ◽  
Atsuko Koyama ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
T Cell ◽  
Protein Kinase ◽  
Cell Leukaemia ◽  
Down Regulation ◽  
Kinase C ◽  
Protein Kinase C Activation

scholarly journals Down-regulation of Na channel α-subunit mRNA by protein kinase C e in adrenal chromaffin cells

1997 ◽  
Vol 73 ◽  
pp. 157
Author(s):  
Toshihiko Yanagita ◽  
Hideyuki Kobayashi ◽  
Keizou Masumoto ◽  
Ryuichi Yamamoto ◽  
Tomoaki Yuhi ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Chromaffin Cells ◽  
Na Channel ◽  
Adrenal Chromaffin Cells ◽  
Down Regulation ◽  
Α Subunit ◽  
Subunit Mrna ◽  
Kinase C ◽  
Adrenal Chromaffin

Down-regulation of protein kinase C and kinase inhibitors dissociate short- and long-term enhancement produced by one-trial conditioning of Hermissenda

1993 ◽  
Vol 69 (2) ◽  
pp. 636-641 ◽  
Author(s):  
T. Crow ◽  
J. Forrester
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase Inhibitors ◽  
Protein Kinase Inhibitors ◽  
Cellular Plasticity ◽  
Short Term ◽  
Down Regulation ◽  
Kinase C ◽  
Short And Long Term

1. The visual system of Hermissenda has been studied extensively as a site of cellular plasticity produced by classical conditioning. Previous research has shown that one-trial conditioning, consisting of light paired with serotonin (5-HT) results in short- and long-term enhancement of light-elicited generator potentials in identified type B-photoreceptors. Recent evidence suggests that 5-HT exerts its effects on the induction of short-term enhancement by activation of protein kinase C (PKC), a Ca(2+)-activated and phospholipid-dependent protein kinase. However, the contribution of protein kinases in general, and specifically PKC in long-term enhancement has not been established. 2. The protein kinase inhibitors H-7 and sphingosine blocked the induction of short-term enhancement when applied before one-trial conditioning. However, the conditions that are sufficient to block the induction of short-term enhancement do not block long-term enhancement. Sphingosine and H-7 do not block the induction and expression of long-term enhancement when applied before one-trial conditioning. 3. Pretreatment before conditioning with 12-O-tetradecanoyl-phorbol-13-acetate (TPA), which leads to down-regulation of PKC, also did not block long-term enhancement. Down-regulation by itself did not produce enhancement, although the transient peak of light-elicited generator potentials was reduced by pretreatment with TPA. 4. The results suggest that the induction of short- and long-term enhancement involve parallel processes, and thus the expression of long-term cellular plasticity produced by one-trial conditioning does not depend on the induction or expression of short-term enhancement.

scholarly journals Invariant Leu Preceding Turn Motif Phosphorylation Site Controls the Interaction of Protein Kinase C with Hsp70

2006 ◽  
Vol 281 (43) ◽  
pp. 32461-32468 ◽  
Author(s):  
Tianyan Gao ◽  
Alexandra C. Newton
Keyword(s):  
Protein Kinase C ◽  
Heat Shock ◽  
Protein Kinase ◽  
Phosphorylation Site ◽  
Insoluble Fraction ◽  
Down Regulation ◽  
Kinase C ◽  
Shock Proteins ◽  
Invariant Residue ◽  
Autophosphorylation Site

Heat shock proteins play important roles in regulating signal transduction in cells by associating with, and stabilizing, diverse signaling molecules, including protein kinases. Previously, we have shown that heat shock protein Hsp70 associates with protein kinase C (PKC) via an interaction that is triggered by dephosphorylation at the turn phosphorylation motif. Here we have identified an invariant residue in the carboxyl terminus of PKC that mediates the binding to Hsp70. Specifically, we show that Hsp70 binds to Leu (Leu-640) immediately preceding the conserved turn motif autophosphorylation site (Thr-641) in PKC βII. Co-immunoprecipitation experiments reveal that mutation of Leu-640 to Gly decreases the interaction of Hsp70 with PKC βII. This weakened interaction between Hsp70 and the mutant PKCs results in accumulation of dephosphorylated PKC in the detergent-insoluble fraction of cells. In addition, the Hsp70-binding mutant is considerably more sensitive to down-regulation compared with WT PKC: disruption of Hsp70 binding leads to accelerated dephosphorylation and enhanced ubiquitination of mutant PKC upon phorbol ester treatment. Last, pulse-chase experiments demonstrate that Hsp70 preferentially binds the species of mature PKC that has become dephosphorylated compared with the newly synthesized protein that has yet to be phosphorylated. Thus, Hsp70 binds a hydrophobic residue preceding the turn motif, protecting PKC from down-regulation and sustaining the signaling lifetime of the kinase.

Sign in / Sign up

Export Citation Format

Share Document