GTC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Genes to Cells (2005) 10, 225-239. doi:10.1111/j.1365-2443.2005.00830.x
© 2005 Blackwell Publishing or its licensors
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Seki, T.
Right arrow Articles by Sakai, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Seki, T.
Right arrow Articles by Sakai, N.

Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC

Takahiro Seki1, Hiroaki Matsubayashi1, Taku Amano1, Yasuhito Shirai2, Naoaki Saito2 and Norio Sakai1,*

1 Department of Molecular and Pharmacological Neuroscience, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima 734-8551, Japan
2 Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe 657-8501, Japan

Protein kinase C (PKC) is translocated to various cellular regions in a subtype and stimulation-dependent manner. Thereafter, the activated PKC phosphorylates its substrate and causes subsequent cellular responses (PKC targeting). The 3-phosphoinositide-dependent protein kinase-1 (PDK1) has an essential role in the maturation of PKC by phosphorylating a threonine residue in the PKC activation loop. To elucidate the role of PDK1 in PKC targeting, we expressed mutant {gamma}- or {delta}-PKC fused with GFP ({gamma}- or {delta}-PKC-ALM (activation loop mutant)-GFP), whose threonine residue in the activation loop was replaced with alanine, and compared their P2Y receptor-mediated translocation with wild-type PKC-GFP in CHO cells. ATP (1 mM) induced the transient translocation of wild-type {gamma}- or {delta}-PKC-GFP from cytoplasm to plasma membrane and following retranslocation from membrane to the cytoplasm. {gamma}- or {delta}-PKC-ALM-GFP was also translocated to plasma membrane, which was, however, retained at the membrane for a longer period than wild type. Similar results were observed in kinase-negative PKC mutants, indicating that the phosphorylation by PDK1 affects the retranslocation step of PKC by regulating the kinase activity. The simultaneous monitoring of [Ca2+]i and diacylglycerol (DG) levels with the translocation of PKC demonstrated that PKC-ALM induced the prolonged accumulation of DG, resulting in the prolonged retention of PKC-ALM at the plasma membrane. It is possible that PKC-ALM with decreased kinase activity could delay the conversion of DG at the plasma membrane. Our present study suggests that the activation loop phosphorylation plays an important role in receptor-mediated PKC targeting.

Communicated by: Kozo Kaibuchi

*Correspondence: E-mail: nsakai{at}hiroshima-u.ac.jp




This article has been cited by other articles:


Home page
 EndocrinologyHome page
E. N. Nierth-Simpson, M. M. Martin, T.-C. Chiang, L. I. Melnik, L. V. Rhodes, S. E. Muir, M. E. Burow, and J. A. McLachlan
Human Uterine Smooth Muscle and Leiomyoma Cells Differ in Their Rapid 17{beta}-Estradiol Signaling: Implications for Proliferation
Endocrinology, May 1, 2009; 150(5): 2436 - 2445.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
B. Balasubramanian, W. Portillo, A. Reyna, J. Z. Chen, A. N. Moore, P. K. Dash, and S. K. Mani
Nonclassical Mechanisms of Progesterone Action in the Brain: I. Protein Kinase C Activation in the Hypothalamus of Female Rats
Endocrinology, November 1, 2008; 149(11): 5509 - 5517.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
J. S. Y. Ma, T. F. Haydar, and S. Radoja
Protein Kinase C {delta} Localizes to Secretory Lysosomes in CD8+ CTL and Directly Mediates TCR Signals Leading to Granule Exocytosis-Mediated Cytotoxicity
J. Immunol., October 1, 2008; 181(7): 4716 - 4722.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
T. Ikegami, L. Krilov, J. Meng, B. Patel, K. Chapin-Kennedy, and B. Bouscarel
Decreased Glucagon Responsiveness by Bile Acids: A Role for Protein Kinase C{alpha} and Glucagon Receptor Phosphorylation
Endocrinology, November 1, 2006; 147(11): 5294 - 5302.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
T. Seki, N. Irie, K. Nakamura, H. Sakaue, W. Ogawa, M. Kasuga, H. Yamamoto, S. Ohmori, N. Saito, and N. Sakai
Fused protein of deltaPKC activation loop and PDK1-interacting fragment (deltaAL-PIF) functions as a pseudosubstrate and an inhibitory molecule for PDK1 when expressed in cells.
Genes Cells, September 1, 2006; 11(9): 1051 - 1070.
[Abstract] [Full Text] [PDF]

Home page
 J. Lipid Res.Home page
L. Brizuela, M. Rabano, A. Pena, P. Gangoiti, J. M. Macarulla, M. Trueba, and A. Gomez-Munoz
Sphingosine 1-phosphate: a novel stimulator of aldosterone secretion
J. Lipid Res., June 1, 2006; 47(6): 1238 - 1249.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Collazos, B. Diouf, N. C. Guerineau, C. Quittau-Prevostel, M. Peter, F. Coudane, F. Hollande, and D. Joubert
A Spatiotemporally Coordinated Cascade of Protein Kinase C Activation Controls Isoform-Selective Translocation.
Mol. Cell. Biol., March 1, 2006; 26(6): 2247 - 2261.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
Copyright © 2005 by Wiley-Blackwell Publishing.