Phorbol Ester Effects in Atypical Protein Kinase C ζ Overexpressing NIH3T3 Cells: Possible Evidence for Crosstalk between Protein Kinase C Isoforms

1997 ◽  
Vol 237 (2) ◽  
pp. 336-339 ◽  
Author(s):  
Soo-Jung Kim ◽  
Yoon-Young Chang ◽  
Shin-Sung Kang ◽  
Jang-Soo Chun
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Atypical Protein Kinase C ◽  
Nih3t3 Cells ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals 663 Differential roles of atypical protein kinase C isoforms in wound healing

2017 ◽  
Vol 137 (10) ◽  
pp. S306
Author(s):  
S. Osada ◽  
N. Noguchi ◽  
T. Hirose ◽  
T. Suzuki ◽  
M. Kagaya ◽  
...  
Keyword(s):  
Wound Healing ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals Targeted Deletion of Protein Kinase C λ Reveals a Distribution of Functions between the Two Atypical Protein Kinase C Isoforms

2004 ◽  
Vol 173 (5) ◽  
pp. 3250-3260 ◽  
Author(s):  
Rachel S. Soloff ◽  
Carol Katayama ◽  
Meei Yun Lin ◽  
James R. Feramisco ◽  
Stephen M. Hedrick
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atypical Protein Kinase C ◽  
Targeted Deletion ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Isoforms

Atypical protein kinase C isoforms differentially regulate directional keratinocyte migration during wound healing

2019 ◽  
Vol 93 (2) ◽  
pp. 101-108 ◽  
Author(s):  
Natsuko Noguchi ◽  
Tomonori Hirose ◽  
Tomoko Suzuki ◽  
Masami Kagaya ◽  
Kazuhiro Chida ◽  
...  
Keyword(s):  
Wound Healing ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Keratinocyte Migration ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals Evidence That Atypical Protein Kinase C-λ and Atypical Protein Kinase C-ζ Participate in Ras-mediated Reorganization of the F-actin Cytoskeleton

1999 ◽  
Vol 144 (3) ◽  
pp. 413-425 ◽  
Author(s):  
Florian Überall ◽  
Karina Hellbert ◽  
Sonja Kampfer ◽  
Karl Maly ◽  
Andreas Villunger ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Actin Cytoskeleton ◽  
Dominant Negative ◽  
Stress Fibers ◽  
Atypical Protein Kinase C ◽  
Nih3t3 Cells ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Actin Stress Fibers

Expression of transforming Ha-Ras L61 in NIH3T3 cells causes profound morphological alterations which include a disassembly of actin stress fibers. The Ras-induced dissolution of actin stress fibers is blocked by the specific PKC inhibitor GF109203X at concentrations which inhibit the activity of the atypical aPKC isotypes λ and ζ, whereas lower concentrations of the inhibitor which block conventional and novel PKC isotypes are ineffective. Coexpression of transforming Ha-Ras L61 with kinase-defective, dominant-negative (DN) mutants of aPKC-λ and aPKC-ζ, as well as antisense constructs encoding RNA-directed against isotype-specific 5′ sequences of the corresponding mRNA, abrogates the Ha-Ras–induced reorganization of the actin cytoskeleton. Expression of a kinase-defective, DN mutant of cPKC-α was unable to counteract Ras with regard to the dissolution of actin stress fibers. Transfection of cells with constructs encoding constitutively active (CA) mutants of atypical aPKC-λ and aPKC-ζ lead to a disassembly of stress fibers independent of oncogenic Ha-Ras. Coexpression of (DN) Rac-1 N17 and addition of the phosphatidylinositol 3′-kinase (PI3K) inhibitors wortmannin and LY294002 are in agreement with a tentative model suggesting that, in the signaling pathway from Ha-Ras to the cytoskeleton aPKC-λ acts upstream of PI3K and Rac-1, whereas aPKC-ζ functions downstream of PI3K and Rac-1. This model is supported by studies demonstrating that cotransfection with plasmids encoding L61Ras and either aPKC-λ or aPKC-ζ results in a stimulation of the kinase activity of both enzymes. Furthermore, the Ras-mediated activation of PKC-ζ was abrogated by coexpression of DN Rac-1 N17.

An Allosteric Inhibitor Scaffold Targeting the PIF-Pocket of Atypical Protein Kinase C Isoforms

2017 ◽  
Vol 12 (2) ◽  
pp. 564-573 ◽  
Author(s):  
Jose M. Arencibia ◽  
Wolfgang Fröhner ◽  
Magdalena Krupa ◽  
Daniel Pastor-Flores ◽  
Piotr Merker ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Allosteric Inhibitor ◽  
Kinase C ◽  
Protein Kinase C Isoforms

scholarly journals MEK5, a New Target of the Atypical Protein Kinase C Isoforms in Mitogenic Signaling

2001 ◽  
Vol 21 (4) ◽  
pp. 1218-1227 ◽  
Author(s):  
Marı́a T. Diaz-Meco ◽  
Jorge Moscat
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Mitogenic Signaling ◽  
Atypical Protein Kinase C ◽  
Interaction Domain ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Mitogen Activated Protein ◽  
Protein Kinase C Isoforms

ABSTRACT The MEK5–extracellular signal-regulated kinase (ERK5) tandem is a novel mitogen-activated protein kinase cassette critically involved in mitogenic activation by the epidermal growth factor (EGF). The atypical protein kinase C isoforms (aPKCs) have been shown to be required for cell growth and proliferation and have been reported to interact with the adapter protein p62 through a short stretch of acidic amino acids termed the aPKC interaction domain. This region is also present in MEK5, suggesting that it may be an aPKC-binding partner. Here we demonstrate that the aPKCs interact in an EGF-inducible manner with MEK5 and that this interaction is required and sufficient for the activation of MEK5 in response to EGF. Consistent with the role of the aPKCs in the MEK5-ERK5 pathway, we show that ζPKC and λ/ιPKC activate the Jun promoter through the MEF2C element, a well-established target of ERK5. From all these results, we conclude that MEK5 is a critical target of the aPKCs during mitogenic signaling.

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