Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print November 3, 2004
Mol. Biol. Cell 10.1091/mbc.E04-05-0426

A more recent version of this article appeared on January 1, 2005
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E04-05-0426v1
16/1/117    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Huang, S.-C.
Right arrow Articles by Benz, E. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, S.-C.
Right arrow Articles by Benz, E. J., Jr.

Submitted on May 21, 2004
Revised on September 29, 2004
Accepted on October 8, 2004

Mitotic Regulation of Protein 4.1R Involves Phosphorylation by cdc2 Kinase

Shu-Ching Huang,*{dagger}{ddagger} Eva S. Liu,* Siu-Hong Chan,{sect} Indira D. Munagala,* Heidi T. Cho,* Ramasamy Jagadeeswaran,* and Edward J. Benz Jr.*{dagger}{sect}||¶#

*Department of Medical Oncology, Dana Farber Cancer Institute, Boston, MA 02115; {dagger}Department of Medicine, Harvard Medical School, Boston, MA 02115; {sect}Department of Medicine, Johns Hopkins University, Baltimore, MD 21205; ||Department of Medicine, Brigham and Women’s Hospital, Boston, MA 02115; Department of Pediatrics, Children’s Hospital of Boston, Boston, MA 02115; #Department of Pathology, Harvard Medical School, Boston, MA 02115

Monitoring Editor: Douglas Koshland

The nonerythrocyte isoform of the cytoskeletal protein 4.1R (4.1R) is associated with morphologically dynamic structures during cell division and has been implicated in mitotic spindle function. In this study, we define important 4.1R isoforms expressed in interphase and mitotic cells by RT-PCR and mini-cDNA library construction. Moreover, we show that 4.1R is phosphorylated by p34cdc2 kinase on residues Thr60 and Ser679 in a mitosis-specific manner. Phosphorylated 4.1R135 isoform(s) associate with tubulin and Nuclear Mitotic Apparatus protein (NuMA) in intact HeLa cells in vivo, as well as with the microtubule-associated proteins in mitotic asters assembled in vitro. Recombinant 4.1R135 is readily phosphorylated in mitotic extracts and reconstitutes mitotic aster assemblies in 4.1R-immunodepleted extracts in vitro. Furthermore, phosphorylation of these residues appears to be essential for the targeting of 4.1R to the spindle poles and for mitotic microtubule aster assembly in vitro. Phosphorylation of 4.1R also enhances its association with NuMA and tubulin. Finally, we used siRNA inhibition to deplete 4.1R from HeLa cells and provide the first direct genetic evidence that 4.1R is required to efficiently focus mitotic spindle poles. Thus, we suggest that 4.1R is a member of the suite of direct cdc2 substrates that are required for the establishment of a bipolar spindle.

{ddagger}Corresponding author. E-mail: shu-ching_huang{at}dfci.harvard.edu




This article has been cited by other articles:


Home page
 FASEB J.Home page
S. Yang, X. Liu, Y. Yin, M. N. Fukuda, and J. Zhou
Tastin is required for bipolar spindle assembly and centrosome integrity during mitosis
FASEB J, June 1, 2008; 22(6): 1960 - 1972.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
G. Yang, S.-C. Huang, J. Y. Wu, and E. J. Benz Jr
Regulated Fox-2 isoform expression mediates protein 4.1R splicing during erythroid differentiation
Blood, January 1, 2008; 111(1): 392 - 401.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2004 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.