scholarly journals Activation of the ERK Pathway and Atypical Protein Kinase C Isoforms in Exercise- and Aminoimidazole-4-carboxamide- 1-β-d-riboside (AICAR)-stimulated Glucose Transport

2002 ◽  
Vol 277 (26) ◽  
pp. 23554-23562 ◽  
Author(s):  
Hubert C. Chen ◽  
Gautam Bandyopadhyay ◽  
Mini P. Sajan ◽  
Yoshinori Kanoh ◽  
Mary Standaert ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Glucose Transport ◽  
Erk Pathway ◽  
Atypical Protein Kinase C ◽  
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

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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