| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 275, Issue 38, 29772-29778, September 22, 2000
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the Diabetes Unit, the Department of Molecular Biology,
Massachusetts General Hospital and the Department of Medicine, Harvard
Medical School, Boston, Massachusetts 02114 and the
§ Diabetes and Metabolism Unit, Boston University Medical
Center, Boston, Massachusetts 02118
14-3-3 proteins bind their targets through a
specific serine/threonine-phosphorylated motif present on the target
protein. This binding is a crucial step in the
phosphorylation-dependent regulation of various key proteins
involved in signal transduction and cell cycle control. We report that
treatment of COS-7 cells with the phosphatase inhibitor calyculin A
induces association of 14-3-3 with a 55-kDa protein, identified as the
intermediate filament protein vimentin. Association of vimentin with
14-3-3 depends on vimentin phosphorylation and requires the
phosphopeptide-binding domain of 14-3-3. The region necessary for
binding to 14-3-3 is confined to the vimentin amino-terminal head
domain (amino acids 1-96). Monomeric forms of 14-3-3 do not bind
vimentin in vivo or in vitro, indicating that a
stable complex requires the binding of a 14-3-3 dimer to two sites on a
single vimentin polypeptide. The calyculin A-induced association of
vimentin with 14-3-3 in vivo results in the displacement of
most other 14-3-3 partners, including the protooncogene Raf, which
nevertheless remain capable of binding 14-3-3 in vitro.
Concomitant with 14-3-3 displacement, calyculin A treatment blocks Raf
activation by EGF; however, this inhibition is completely overcome by
14-3-3 overexpression in vivo or by the addition of
prokaryotic recombinant 14-3-3 in vitro. Thus,
phosphovimentin, by sequestering 14-3-3 and limiting its availability
to other target proteins can affect intracellular signaling processes
that require 14-3-3.
Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo*
,
*
This work was supported by a grant from Eli Lilly Inc.The costs of publication of this
article were defrayed in part by the payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Cardiovascular
Research Institute, Division of Molecular Cardiology, The Texas A&M
University System, Health Science Center, College of Medicine, 1901 S. 1st St., Bldg. 162, Temple, TX 76504. Tel.: 254-778-4811 (ext. 1327);
Fax: 254-899-6498; E-mail: tzivion@medicine.tamu.edu.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Kim and P. A. Coulombe Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm Genes & Dev., July 1, 2007; 21(13): 1581 - 1597. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H.-M. Pallari and J. E. Eriksson Intermediate Filaments as Signaling Platforms Sci. Signal., December 19, 2006; 2006(366): pe53 - pe53. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Li, Y. Guo, J. Teng, M. Ding, A. C. H. Yu, and J. Chen 14-3-3{gamma} affects dynamics and integrity of glial filaments by binding to phosphorylated GFAP J. Cell Sci., November 1, 2006; 119(21): 4452 - 4461. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. Shen and S. C. Huber Polycations Globally Enhance Binding of 14-3-3{omega} to Target Proteins in Spinach Leaves Plant Cell Physiol., June 1, 2006; 47(6): 764 - 771. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Zhu, V. Balan, A. Bronisz, K. Balan, H. Sun, D. T. Leicht, Z. Luo, J. Qin, J. Avruch, and G. Tzivion Identification of Raf-1 S471 as a Novel Phosphorylation Site Critical for Raf-1 and B-Raf Kinase Activities and for MEK Binding Mol. Biol. Cell, October 1, 2005; 16(10): 4733 - 4744. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Bridges and G. B. G. Moorhead 14-3-3 Proteins: A Number of Functions for a Numbered Protein Sci. Signal., August 9, 2005; 2005(296): re10 - re10. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N.-O. Ku, H. Fu, and M. B. Omary Raf-1 activation disrupts its binding to keratins during cell stress J. Cell Biol., August 16, 2004; 166(4): 479 - 485. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J.-i. Satoh, T. Yamamura, and K. Arima The 14-3-3 Protein {epsilon} Isoform Expressed in Reactive Astrocytes in Demyelinating Lesions of Multiple Sclerosis Binds to Vimentin and Glial Fibrillary Acidic Protein in Cultured Human Astrocytes Am. J. Pathol., August 1, 2004; 165(2): 577 - 592. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Bridges and G. B. G. Moorhead 14-3-3 Proteins: A Number of Functions for a Numbered Protein Sci. Signal., July 20, 2004; 2004(242): re10 - re10. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. E. Eriksson, T. He, A. V. Trejo-Skalli, A.-S. Harmala-Brasken, J. Hellman, Y.-H. Chou, and R. D. Goldman Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments J. Cell Sci., February 22, 2004; 117(6): 919 - 932. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. H. Shen, J. Godlewski, A. Bronisz, J. Zhu, M. J. Comb, J. Avruch, and G. Tzivion Significance of 14-3-3 Self-Dimerization for Phosphorylation-dependent Target Binding Mol. Biol. Cell, November 1, 2003; 14(11): 4721 - 4733. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Agarwal-Mawal, H. Y. Qureshi, P. W. Cafferty, Z. Yuan, D. Han, R. Lin, and H. K. Paudel 14-3-3 Connects Glycogen Synthase Kinase-3beta to Tau within a Brain Microtubule-associated Tau Phosphorylation Complex J. Biol. Chem., April 4, 2003; 278(15): 12722 - 12728. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N.-O. Ku, S. Michie, E. Z. Resurreccion, R. L. Broome, and M. B. Omary Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression PNAS, April 2, 2002; 99(7): 4373 - 4378. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Tzivion and J. Avruch 14-3-3 Proteins: Active Cofactors in Cellular Regulation by Serine/Threonine Phosphorylation J. Biol. Chem., January 25, 2002; 277(5): 3061 - 3064. [Full Text] [PDF]
|
|
|
|
 |
|
 H. Weiner and W. M. Kaiser Antibodies to assess phosphorylation of spinach leaf nitrate reductase on serine 543 and its binding to 14-3-3 proteins J. Exp. Bot., June 1, 2001; 52(359): 1165 - 1172. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Waelter, A. Boeddrich, R. Lurz, E. Scherzinger, G. Lueder, H. Lehrach, and E. E. Wanker Accumulation of Mutant Huntingtin Fragments in Aggresome-like Inclusion Bodies as a Result of Insufficient Protein Degradation Mol. Biol. Cell, May 1, 2001; 12(5): 1393 - 1407. [Abstract] [Full Text]
|
|
|
|
 |
|
 C.-W. Chiang, G. Harris, C. Ellig, S. C. Masters, R. Subramanian, S. Shenolikar, B. E. Wadzinski, and E. Yang Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin- 3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation Blood, March 1, 2001; 97(5): 1289 - 1297. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. M. Sahlgren, A. Mikhailov, J. Hellman, Y.-H. Chou, U. Lendahl, R. D. Goldman, and J. E. Eriksson Mitotic Reorganization of the Intermediate Filament Protein Nestin Involves Phosphorylation by cdc2 Kinase J. Biol. Chem., May 4, 2001; 276(19): 16456 - 16463. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N.-O. Ku, S. Michie, E. Z. Resurreccion, R. L. Broome, and M. B. Omary Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression PNAS, April 2, 2002; 99(7): 4373 - 4378. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
