scholarly journals Targeting of Protein Kinase Cα to Caveolae

1998 ◽  
Vol 141 (3) ◽  
pp. 601-610 ◽  
Author(s):  
Chieko Mineo ◽  
Yun-Shu Ying ◽  
Christine Chapline ◽  
Susan Jaken ◽  
Richard G.W. Anderson
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Regulatory Domain ◽  
Calcium Dependent ◽  
High Affinity ◽  
Membrane Invagination ◽  
Protein Kinase Cα ◽  
Flanking Sequences ◽  
Modulate Signal ◽  
Regulatory Functions

Previously, we showed caveolae contain a population of protein kinase Cα (PKCα) that appears to regulate membrane invagination. We now report that multiple PKC isoenzymes are enriched in caveolae of unstimulated fibroblasts. To understand the mechanism of PKC targeting, we prepared caveolae lacking PKCα and measured the interaction of recombinant PKCα with these membranes. PKCα bound with high affinity and specificity to caveolae membranes. Binding was calcium dependent, did not require the addition of factors that activate the enzyme, and involved the regulatory domain of the molecule. A 68-kD PKCα-binding protein identified as sdr (serum deprivation response) was isolated by interaction cloning and localized to caveolae. Antibodies against sdr inhibited PKCα binding. A 100–amino acid sequence from the middle of sdr competitively blocked PKCα binding while flanking sequences were inactive. Caveolae appear to be a membrane site where PKC enzymes are organized to carry out essential regulatory functions as well as to modulate signal transduction at the cell surface.

A calcium-dependent protein kinase with a regulatory domain similar to calmodulin

Science ◽  
1991 ◽  
Vol 252 (5008) ◽  
pp. 951-954 ◽  
Author(s):  
J. Harper ◽  
M. Sussman ◽  
G. Schaller ◽  
C Putnam-Evans ◽  
H Charbonneau ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Regulatory Domain ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinase

scholarly journals Intracellular cleavage of glycosylphosphatidylinositol by phospholipase D induces activation of protein kinase Cα

1999 ◽  
Vol 342 (2) ◽  
pp. 449-455 ◽  
Author(s):  
Hiroshi TSUJIOKA ◽  
Noboru TAKAMI ◽  
Yoshio MISUMI ◽  
Yukio IKEHARA
Keyword(s):  
Signal Transduction ◽  
Endoplasmic Reticulum ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Secretory Pathway ◽  
Gradient Centrifugation ◽  
Endoplasmic Reticulum Membrane ◽  
Gpi Anchor ◽  
Protein Kinase Cα ◽  
In Cells

Many proteins are anchored to the cell membrane by glycosylphosphatidylinositol (GPI). One of the functions proposed for the GPI anchor is as a possible mediator in signal transduction through its hydrolysis. GPI-specific phospholipase D (GPI-PLD) is a secretory protein that is suggested to be involved in the release of GPI-anchored protein from the membrane. In the present study we examined how GPI-PLD is involved in signal transduction. When introduced exogenously and overexpressed in cells, GPI-PLD cleaved the GPI anchors in the early secretory pathway, possibly in the endoplasmic reticulum, resulting in an increased production of diacylglycerol. Experiments in vitro and in vivo showed that the association of protein kinase Cα (PKCα) with membranes was increased markedly by expression of GPI-PLD in cells. Furthermore, sucrose-density-gradient centrifugation and immunofluorescence microscopy demonstrated that PKCα was translocated to the endoplasmic reticulum membrane in cells expressing GPI-PLD, in contrast with its association with the plasma membrane in cells treated with PMA. We also confirmed that the phosphorylation of c-Fos as well as PKCα itself was greatly enhanced by the expression of GPI-PLD. Taken together, these results suggest that GPI-PLD is involved in intracellular cleavage of the GPI anchor, which is a new potential source of diacylglycerol production to activate PKCα.

scholarly journals Regulation of wound-responsive calcium-dependent protein kinase from maize (ZmCPK11) by phosphatidic acid.

2011 ◽  
Vol 58 (4) ◽  
Author(s):  
Maria Klimecka ◽  
Jadwiga Szczegielniak ◽  
Luiza Godecka ◽  
Elżbieta Lewandowska-Gnatowska ◽  
Grażyna Dobrowolska ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Phosphatidic Acid ◽  
Transcript Level ◽  
Lipid Binding ◽  
Pcr Analysis ◽  
Dependent Protein Kinase ◽  
Calcium Dependent ◽  
Dependent Protein ◽  
Calcium Dependent Protein Kinase

In plant cells, phospholipids are not only membrane components but also act as second messengers interacting with various proteins and regulating diverse cellular processes, including stress signal transduction. Here, we report studies on the effects of various phospholipids on the activity and expression of maize wound-responsive calcium-dependent protein kinase (ZmCPK11). Our results revealed that in leaves treated with n-butanol, a potent inhibitor of phosphatidic acid (PA) synthesis catalyzed by phospholipase D, a significant decrease of ZmCPK11 activity was observed, indicating contribution of PA in the kinase activation. Using lipid binding assays, we demonstrate that among various phospholipids only saturated acyl species (16:0 and 18:0) of phosphatidic acid are able to bind to ZmCPK11. Saturated acyl species of PA are also able to stimulate phosphorylation of exogenous substrates by ZmCPK11 and autophosphorylation of the kinase. The level of ZmCPK11 autophosphorylation is correlated with its enzymatic activity. RT-PCR analysis showed that transcript level of ZmCPK11 in maize leaves increased in response to PA treatment. The influence of PA on the activity and transcript level of ZmCPK11 suggests an involvement of this kinase in a PA-mediated wound signal transduction pathway.

scholarly journals Cytoskeletal Active Drugs Modulate Signal Transduction in the Protein Kinase C Pathway.

1993 ◽  
Vol 18 (3) ◽  
pp. 151-160 ◽  
Author(s):  
Grace K. Pavlath ◽  
Yoshiko Shimizu ◽  
Nobuyoshi Shimizu
Keyword(s):  
Signal Transduction ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Modulate Signal

Role of protein kinase Cα in melatonin signal transduction

2006 ◽  
Vol 252 (1-2) ◽  
pp. 82-87 ◽  
Author(s):  
S.R. Sampson ◽  
Z. Lupowitz ◽  
L. Braiman ◽  
N. Zisapel
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase Cα
Sign in / Sign up

Export Citation Format

Share Document