HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chou, Y. H. Articles by Goldman, R. Search for Related Content PubMed PubMed Citation Articles by Chou, Y. H. Articles by Goldman, R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 12, 7325-7328, Apr, 1991

The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site

YH Chou, KL Ngai and R Goldman
Department of Cell, Molecular, and Structural Biology, Northwestern University, Chicago, Illinois 60611.

The disassembly of vimentin-containing intermediate filament (IF) networks during mitosis in BHK-21 cells is accompanied by increased phosphorylation of vimentin (Chou, Y.-H., Rosevear, E., and Goldman, R. D. (1989) Proc. Natl. Acad. Sci. U. S. A. 86, 1885-1889). We have recently identified p34cdc2 as the catalytic subunit of one of the two endogenous vimentin kinases in mitotic baby hamster kidney cells (Chou, Y.-H., Bischoff, J. R., Beach, D., and Goldman, R. D. (1990) Cell 62, 1063-1071). To begin to characterize the biochemical basis of the p34cdc2-mediated IF disassembly process, we have purified and sequenced the 32P-labeled tryptic peptides derived from in vitro-phosphorylated vimentin. The results demonstrate that Ser-55, in the N-terminal non- alpha-helical domain of vimentin, is the most favored phosphorylation site. This finding supports the idea that the N-terminal domain of type III IF protein plays a crucial role in regulating IF structure and supramolecular organization.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. Yamaguchi, H. Goto, T. Yokoyama, H. Sillje, A. Hanisch, A. Uldschmid, Y. Takai, T. Oguri, E. A. Nigg, and M. Inagaki Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis J. Cell Biol., November 7, 2005; 171(3): 431 - 436. [Abstract] [Full Text] [PDF]

				S. Stefanovic, M. Windsor, K.-i. Nagata, M. Inagaki, and T. Wileman Vimentin Rearrangement during African Swine Fever Virus Infection Involves Retrograde Transport along Microtubules and Phosphorylation of Vimentin by Calcium Calmodulin Kinase II J. Virol., September 15, 2005; 79(18): 11766 - 11775. [Abstract] [Full Text] [PDF]

				S. Ermakova, B. Y. Choi, H. S. Choi, B. S. Kang, A. M. Bode, and Z. Dong The Intermediate Filament Protein Vimentin Is a New Target for Epigallocatechin Gallate J. Biol. Chem., April 29, 2005; 280(17): 16882 - 16890. [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]

				P. JANOSCH, A. KIESER, M. EULITZ, J. LOVRIC, G. SAUER, M. REICHERT, F. GOUNARI, D. BÜSCHER, M. BACCARINI, H. MISCHAK, et al. The Raf-1 kinase associates with vimentin kinases and regulates the structure of vimentin filaments FASEB J, October 1, 2000; 14(13): 2008 - 2021. [Abstract] [Full Text]

				P. Vilalta, L Zhang, and S. Hamm-Alvarez A novel taxol-induced vimentin phosphorylation and stabilization revealed by studies on stable microtubules and vimentin intermediate filaments J. Cell Sci., January 7, 1998; 111(13): 1841 - 1852. [Abstract] [PDF]

				J. Bridger, H Herrmann, C Munkel, and P Lichter Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin J. Cell Sci., January 5, 1998; 111(9): 1241 - 1253. [Abstract] [PDF]

				N. Malecz, R. Foisner, C. Stadler, and G. Wiche Identification of Plectin as a Substrate of p34[IMAGE]Kinase and Mapping of a Single Phosphorylation Site J. Biol. Chem., April 5, 1996; 271(14): 8203 - 8208. [Abstract] [Full Text] [PDF]

				Y. Chou, P Opal, R. Quinlan, and R. Goldman The relative roles of specific N- and C-terminal phosphorylation sites in the disassembly of intermediate filament in mitotic BHK-21 cells J. Cell Sci., January 4, 1996; 109(4): 817 - 826. [Abstract] [PDF]

				J. E. Ralton, X. Lu, A. M. Hutcheson, and R. A. Quinlan Identification of two N-terminal non-alpha-helical domain motifs important in the assembly of glial fibrillary acidic protein J. Cell Sci., July 1, 1994; 107(7): 1935 - 1948. [Abstract] [PDF]

				G. Tzivion, Z.-J. Luo, and J. Avruch Calyculin A-induced Vimentin Phosphorylation Sequesters 14-3-3 and Displaces Other 14-3-3 Partners in Vivo J. Biol. Chem., September 15, 2000; 275(38): 29772 - 29778. [Abstract] [Full Text] [PDF]