![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on November 1, 2004
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on July 10, 2004
Revised on August 24, 2004
Accepted on August 25, 2004
Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011; and Section of Molecular and Cellular Biology, University of California at Davis, Davis, CA 95616
Monitoring Editor: Joseph Gall
We have used immunocytochemistry and cross-immunoprecipitation analysis to demonstrate that Megator (Bx34 antigen), a Tpr ortholog in Drosophila with an extended coiled-coil domain, colocalizes with the putative spindle matrix proteins Skeletor and Chromator during mitosis. Analysis of P element mutations in the Megator locus showed that Megator is an essential protein. During interphase, Megator is localized to the nuclear rim and occupies the intranuclear space surrounding the chromosomes. However, during mitosis Megator reorganizes and aligns together with Skeletor and Chromator into a fusiform spindle structure. The Megator metaphase spindle persists in the absence of microtubule spindles, strongly implying that the existence of the Megator-defined spindle does not require polymerized microtubules. Deletion construct analysis in S2 cells indicates that the COOH-terminal part of Megator without the coiled-coil region was sufficient for both nuclear as well as spindle localization. In contrast, the NH2-terminal coiled-coil region remains in the cytoplasm; however, we show that it is capable of assembling into spherical structures. Based on these findings we propose that the COOH-terminal domain of Megator functions as a targeting and localization domain whereas the NH2-terminal domain is responsible for forming polymers that may serve as a structural basis for the putative spindle matrix complex.
Corresponding author.
E-mail: kristen{at}iastate.edu
This article has been cited by other articles:
|
|
 |
|
  K. R. Katsani, R. E. Karess, N. Dostatni, and V. Doye In Vivo Dynamics of Drosophila Nuclear Envelope Components Mol. Biol. Cell, September 1, 2008; 19(9): 3652 - 3666. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Fabian, X. Xia, D. V. Venkitaramani, K. M. Johansen, J. Johansen, D. J. Andrew, and A. Forer Titin in insect spermatocyte spindle fibers associates with microtubules, actin, myosin and the matrix proteins skeletor, megator and chromator J. Cell Sci., July 1, 2007; 120(13): 2190 - 2204. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Jacob, C. Mongkolsiriwatana, K. M. Veley, S. Y. Kim, and S. D. Michaels The Nuclear Pore Protein AtTPR Is Required for RNA Homeostasis, Flowering Time, and Auxin Signaling Plant Physiology, July 1, 2007; 144(3): 1383 - 1390. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. M. Xu, A. Rose, S. Muthuswamy, S. Y. Jeong, S. Venkatakrishnan, Q. Zhao, and I. Meier NUCLEAR PORE ANCHOR, the Arabidopsis Homolog of Tpr/Mlp1/Mlp2/Megator, Is Involved in mRNA Export and SUMO Homeostasis and Affects Diverse Aspects of Plant Development PLANT CELL, May 1, 2007; 19(5): 1537 - 1548. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. N. Cytrynbaum, P. Sommi, I. Brust-Mascher, J. M. Scholey, and A. Mogilner Early Spindle Assembly in Drosophila Embryos: Role of a Force Balance Involving Cytoskeletal Dynamics and Nuclear Mechanics Mol. Biol. Cell, October 1, 2005; 16(10): 4967 - 4981. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Niepel, C. Strambio-de-Castillia, J. Fasolo, B. T. Chait, and M. P. Rout The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly J. Cell Biol., July 18, 2005; 170(2): 225 - 235. [Abstract] [Full Text] [PDF]
|
|
