Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on September 9, 2005
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
280/36/31714    most recent
M506225200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Harada, Y.
Right arrow Articles by Fukada, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Harada, Y.
Right arrow Articles by Fukada, Y.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print June 24, 2005
J. Biol. Chem, 10.1074/jbc.M506225200
Submitted on June 8, 2005
Accepted on June 24, 2005

SER557-phosphorylated mCRY2 is degraded upon synergistic phosphorylation by GSK-3beta

Yuko Harada, Mihoko Sakai, Nobuhiro Kurabayashi, Tsuyoshi Hirota, and Yoshitaka Fukada

Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033

Corresponding Author: sfukada{at}mail.ecc.u-tokyo.ac.jp

Cryptochrome1 and 2 act as essential components of the central and peripheral circadian clocks for generation of circadian rhythms in mammals. Here we show that mouse Cryptochrome2 (mCRY2) is phosphorylated at Ser557 in the liver, a well-characterized peripheral clock tissue. The Ser557-phosphorylated form accumulates in the liver during (subjective) night in parallel with mCRY2 protein, and the phosphorylated form reaches its maximal level at late night preceding the peak-time of the protein abundance by approximately 4 h in both light-dark cycle and constant dark conditions. The Ser557-phosphorylated form of mCRY2 is localized in the nucleus, whereas mCRY2 protein is located in both the cytoplasm and nucleus. Importantly, phosphorylation of mCRY2 at Ser557 allows subsequent phosphorylation at Ser553 by glycogen synthase kinase-3beta (GSK-3beta ), resulting in efficient degradation of mCRY2 by a proteasome pathway. As assessed by phosphorylation of GSK-3beta at Ser9 which negatively regulates the kinase activity, GSK-3beta exhibits a circadian rhythm in its activity with a peak from late night to early morning when Ser557 of mCRY2 is highly phosphorylated. Altogether, the present study demonstrates an important role of sequential phosphorylation at Ser557/Ser553 for destabilization of mCRY2, and illustrates a model that the circadian regulation of mCRY2 phosphorylation contributes to rhythmic degradation of mCRY2 protein.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Hirota, W. G. Lewis, A. C. Liu, J. W. Lee, P. G. Schultz, and S. A. Kay
A chemical biology approach reveals period shortening of the mammalian circadian clock by specific inhibition of GSK-3{beta}
PNAS, December 30, 2008; 105(52): 20746 - 20751.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
X. Yu, D. Shalitin, X. Liu, M. Maymon, J. Klejnot, H. Yang, J. Lopez, X. Zhao, K. T. Bendehakkalu, and C. Lin
Derepression of the NC80 motif is critical for the photoactivation of Arabidopsis CRY2
PNAS, April 24, 2007; 104(17): 7289 - 7294.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
K. Roybal, D. Theobold, A. Graham, J. A. DiNieri, S. J. Russo, V. Krishnan, S. Chakravarty, J. Peevey, N. Oehrlein, S. Birnbaum, et al.
From the Cover: Mania-like behavior induced by disruption of CLOCK
PNAS, April 10, 2007; 104(15): 6406 - 6411.
[Abstract] [Full Text] [PDF]

Home page
 Cold Spring Harb Symp Quant BiolHome page
F. Tamanini, I. Chaves, M. I. Bajek, and G. T. J. van der Horst
Structure Function Analysis of Mammalian Cryptochromes
Cold Spring Harb Symp Quant Biol, January 1, 2007; 72(0): 133 - 139.
[Abstract] [PDF]

Home page
 Cold Spring Harb Symp Quant BiolHome page
K. Vanselow and A. Kramer
Role of Phosphorylation in the Mammalian Circadian Clock
Cold Spring Harb Symp Quant Biol, January 1, 2007; 72(0): 167 - 176.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
M.-J. Boucher, L. Selander, L. Carlsson, and H. Edlund
Phosphorylation Marks IPF1/PDX1 Protein for Degradation by Glycogen Synthase Kinase 3-dependent Mechanisms
J. Biol. Chem., March 10, 2006; 281(10): 6395 - 6403.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement