Membrane Interaction and Protein Kinase C-C1 Domain Binding Properties of 4-Hydroxy-3-(hydroxymethyl) Phenyl Ester Analogues

2014 ◽  
Vol 118 (27) ◽  
pp. 7541-7553 ◽  
Author(s):  
Dipjyoti Talukdar ◽  
Subhankar Panda ◽  
Rituparna Borah ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phenyl Ester ◽  
Binding Properties ◽  
Membrane Interaction ◽  
Kinase C ◽  
C1 Domain

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.

Bilayer interaction and protein kinase C-C1 domain binding studies of kojic acid esters

RSC Advances ◽  
2014 ◽  
Vol 4 (49) ◽  
pp. 25520-25531 ◽  
Author(s):  
Rituparna Borah ◽  
Dipjyoti Talukdar ◽  
Sukhamoy Gorai ◽  
Dipankar Bain ◽  
Debasis Manna
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Lipid Bilayer ◽  
Acid Ester ◽  
Kojic Acid ◽  
Binding Studies ◽  
Binding Properties ◽  
Kinase C ◽  
C1 Domain ◽  
Acid Esters

Synthesis of kojic acid ester analogues and their lipid bilayer interaction and PKC-C1 domain binding properties have been demonstrated in this present work.

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

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 Protein Kinase C Phosphomimetics Alter Thin Filament Ca2+ Binding Properties

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e86279 ◽  
Author(s):  
Bin Liu ◽  
Joseph J. Lopez ◽  
Brandon J. Biesiadecki ◽  
Jonathan P. Davis
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Thin Filament ◽  
Binding Properties ◽  
Kinase C

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.

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