spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Full Text (PDF)
Right arrow References
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Saredi, A.
Right arrow Articles by Compton, D. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saredi, A.
Right arrow Articles by Compton, D. A.

Journal of Cell Science, Vol 110, Issue 11 1287-1297, Copyright © 1997 by Company of Biologists

JOURNAL ARTICLES

Phosphorylation regulates the assembly of NuMA in a mammalian mitotic extract

A Saredi, L Howard and DA Compton
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.

NuMA is a 236 kDa nuclear protein that is required for the organization of the mitotic spindle. To determine how NuMA redistributes in the cell during mitosis, we have examined the behavior of NuMA in a mammalian mitotic extract under conditions conducive to the reassembly of interphase nuclei. NuMA is a soluble protein in mitotic extracts prepared from synchronized cultured cells, but forms insoluble structures when the extract becomes non-mitotic (as judged by the inactivation of cdc2/cyclin B kinase and the disappearance of mpm-2-reactive antigens). These NuMA-containing structures are irregularly shaped particles of 1-2 microm in diameter and their assembly is specific because other nuclear components such as the lamins remain soluble in the extract under these conditions. NuMA is dephosphorylated during this assembly process, and the assembly of these NuMA-containing structures is catalyzed by protein dephosphorylation because protein kinase inhibitors enhance their formation and protein phosphatase inhibitors block their formation. Finally, immunodepletion demonstrates that NuMA is an essential structural component of these insoluble particles, and electron microscopy shows that the particles are composed of a complex interconnected network of foci. These results demonstrate that phosphorylation regulates the solubility of NuMA in a mammalian mitotic extract, and the spontaneous assembly of NuMA into extensive structures upon dephosphorylation supports the conclusion that NuMA serves a structural function.


This article has been cited by other articles:


Home page
 J Exp BotHome page
R. Samaniego, S. Y. Jeong, C. de la Torre, I. Meier, and S. M. Diaz de la Espina
CK2 phosphorylation weakens 90 kDa MFP1 association to the nuclear matrix in Allium cepa
J. Exp. Bot., January 1, 2006; 57(1): 113 - 124.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
O. Kisurina-Evgenieva, G. Mack, Q. Du, I. Macara, A. Khodjakov, and D. A. Compton
Multiple mechanisms regulate NuMA dynamics at spindle poles
J. Cell Sci., December 15, 2004; 117(26): 6391 - 6400.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
M. Novatchkova and F. Eisenhaber
A CH domain-containing N terminus in NuMA?
Protein Sci., October 1, 2002; 11(10): 2281 - 2284.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
M. B. Gordon, L. Howard, and D. A. Compton
Chromosome Movement in Mitosis Requires Microtubule Anchorage at Spindle Poles
J. Cell Biol., January 29, 2001; 152(3): 425 - 434.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
A. Merdes, R. Heald, K. Samejima, W. C. Earnshaw, and D. W. Cleveland
Formation of Spindle Poles by Dynein/Dynactin-dependent Transport of NuMA
J. Cell Biol., May 15, 2000; 149(4): 851 - 862.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
D Lourim and G Krohne
Chromatin binding and polymerization of the endogenous Xenopus egg lamins: the opposing effects of glycogen and ATP
J. Cell Sci., June 14, 1999; 111(24): 3675 - 3686.
[Abstract] [PDF]

Home page
 BloodHome page
A. Melnick and J. D. Licht
Deconstructing a Disease: RAR{alpha}, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia
Blood, May 15, 1999; 93(10): 3167 - 3215.
[Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C.-Y. F. Huang, C.-P. B. Chang, C.-L. Huang, and J. E. Ferrell Jr.
M Phase Phosphorylation of Cytoplasmic Dynein Intermediate Chain and p150Glued
J. Biol. Chem., May 14, 1999; 274(20): 14262 - 14269.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
O. Zatsepina, A Rousselet, P. Chan, M. Olson, E. Jordan, and M Bornens
The nucleolar phosphoprotein B23 redistributes in part to the spindle poles during mitosis
J. Cell Sci., January 2, 1999; 112(4): 455 - 466.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
D. Compton
Focusing on spindle poles
J. Cell Sci., January 6, 1998; 111(11): 1477 - 1481.
[Abstract] [PDF]

Home page
 J. Cell Sci.Home page
A Merdes and D. Cleveland
The role of NuMA in the interphase nucleus
J. Cell Sci., January 1, 1998; 111(1): 71 - 79.
[Abstract] [PDF]


© The Company of Biologists Ltd 1997