The C1 and C2 Domains of Protein Kinase C Are Independent Membrane Targeting Modules, with Specificity for Phosphatidylserine Conferred by the C1 Domain†

Biochemistry ◽  
2000 ◽  
Vol 39 (37) ◽  
pp. 11360-11369 ◽  
Author(s):  
Joanne E. Johnson ◽  
Jennifer Giorgione ◽  
Alexandra C. Newton
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Targeting ◽  
C2 Domains ◽  
Kinase C ◽  
C1 Domain

Alkyl cinnamates as regulator for the C1 domain of protein kinase C isoforms

2012 ◽  
Vol 165 (3) ◽  
pp. 320-330 ◽  
Author(s):  
Narsimha Mamidi ◽  
Sukhamoy Gorai ◽  
Jashobanta Sahoo ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
C1 Domain ◽  
Protein Kinase C Isoforms

scholarly journals Membrane Targeting and Cytoplasmic Sequestration in the Spatiotemporal Localization of Human Protein Kinase C α

2000 ◽  
Vol 275 (8) ◽  
pp. 6014-6021 ◽  
Author(s):  
Alice Vallentin ◽  
Corinne Prévostel ◽  
Teddy Fauquier ◽  
Xavier Bonnefont ◽  
Dominique Joubert
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Protein ◽  
Membrane Targeting ◽  
Kinase C ◽  
Human Protein Kinase ◽  
Spatiotemporal Localization

The C1 Domain of Protein Kinase C as a Lipid Bilayer Surface Sensing Module†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10334-10341 ◽  
Author(s):  
Cojen Ho ◽  
Simon J. Slater ◽  
Brigid Stagliano ◽  
Christopher D. Stubbs
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Kinase C ◽  
Surface Sensing ◽  
C1 Domain

scholarly journals Mechanism of inhibition of protein kinase C by 14-3-3 isoforms. 14-3-3 isoforms do not have phospholipase A2 activity.

1994 ◽  
Vol 299 (3) ◽  
pp. 853-861 ◽  
Author(s):  
K Robinson ◽  
D Jones ◽  
Y Patel ◽  
H Martin ◽  
J Madrazo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase A2 ◽  
Kinase C ◽  
Mechanism Of Inhibition ◽  
C1 Domain ◽  
Novel Method ◽  
Original Observation ◽  
Cytosolic Pla2 ◽  
Phospholipase A2 Activity

The ability of individual members of the 14-3-3 protein family to inhibit protein kinase C (PKC) has been studied by using a synthetic peptide based on the specific 80 kDa substrate for PKC (MARCKS protein) in two different assay systems. Recombinant 14-3-3 and isoforms renatured by a novel method after separation by reverse-phase h.p.l.c. were studied. The detailed effects of diacylglycerol and the phorbol ester phorbol 12-myristate 13-acetate on the inhibition were also investigated. This suggests that one of the sites of interaction of 14-3-3 may be the cysteine-rich (C1) domain in PKC. Since a region in secreted phospholipase A2 (PLA2) shares similarity with this domain, the ability of 14-3-3 to interact with mammalian PLA2 was studied. Cytosolic PLA2 has some similarity to the C2 region of PKC, and the effect of 14-3-3 on this class of PLA2 was also analysed. In contrast with a previous report, no PLA2 activity was found in brain 14-3-3, nor in any of the recombinant proteins tested. These include zeta 14-3-3 isoform, on which the original observation was made.

Synthesis and protein kinase C (PKC)-C1 domain binding properties of diacyltetrol based anionic lipids

2014 ◽  
Vol 10 (11) ◽  
pp. 3002-3013 ◽  
Author(s):  
Narsimha Mamidi ◽  
Subhankar Panda ◽  
Rituparna Borah ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Binding Specificity ◽  
Binding Properties ◽  
Kinase C ◽  
P Protein ◽  
C1 Domain ◽  
Anionic Lipids

Protein kinase C-C1 domain binding specificity of the anionic hybrid lipids.

NPC 15437 interacts with the C1 domain of protein kinase C An analysis using mutant PKC constructs

FEBS Letters ◽  
1991 ◽  
Vol 285 (1) ◽  
pp. 120-123 ◽  
Author(s):  
James P. Sullivan ◽  
Jane R. Connor ◽  
Carol Tiffany ◽  
Barry G. Shearer ◽  
Ronald M. Burch
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
C1 Domain

scholarly journals 14–3-3 Inhibits the Dictyostelium Myosin II Heavy-Chain-specific Protein Kinase C Activity by a Direct Interaction: Identification of the 14–3-3 Binding Domain

1997 ◽  
Vol 8 (10) ◽  
pp. 1889-1899 ◽  
Author(s):  
Meirav Matto-Yelin ◽  
Alastair Aitken ◽  
Shoshana Ravid
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Myosin Ii ◽  
Direct Interaction ◽  
Specific Protein ◽  
Kinase C ◽  
C1 Domain ◽  
Specific Protein Kinase

Myosin II heavy chain (MHC) specific protein kinase C (MHC-PKC), isolated from Dictyostelium discoideum, regulates myosin II assembly and localization in response to the chemoattractant cyclic AMP. Immunoprecipitation of MHC-PKC revealed that it resides as a complex with several proteins. We show herein that one of these proteins is a homologue of the 14–3-3 protein (Dd14–3-3). This protein has recently been implicated in the regulation of intracellular signaling pathways via its interaction with several signaling proteins, such as PKC and Raf-1 kinase. We demonstrate that the mammalian 14–3-3 ζ isoform inhibits the MHC-PKC activity in vitro and that this inhibition is carried out by a direct interaction between the two proteins. Furthermore, we found that the cytosolic MHC-PKC, which is inactive, formed a complex with Dd14–3-3 in the cytosol in a cyclic AMP-dependent manner, whereas the membrane-bound active MHC-PKC was not found in a complex with Dd14–3-3. This suggests that Dd14–3-3 inhibits the MHC-PKC in vivo. We further show that MHC-PKC binds Dd14–3-3 as well as 14–3-3ζ through its C1 domain, and the interaction between these two proteins does not involve a peptide containing phosphoserine as was found for Raf-1 kinase. Our experiments thus show an in vivo function for a member of the 14–3-3 family and demonstrate that MHC-PKC interacts directly with Dd14–3-3 and 14–3-3ζ through its C1 domain both in vitro and in vivo, resulting in the inhibition of the kinase.

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