English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Functional analysis of centrosomal kinase substrates in Drosophila melanogaster reveals a new function of the nuclear envelope component otefin in cell cycle progression

Habermann, K., Mirgorodskaya, E., Gobom, J., Lehmann, V., Müller, H., Blümlein, K., et al. (2012). Functional analysis of centrosomal kinase substrates in Drosophila melanogaster reveals a new function of the nuclear envelope component otefin in cell cycle progression. Molecular and Cellular Biology (Washington, DC), 32(17), 3554-3569. doi:10.1128/MCB.00814-12.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F049-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F04A-7
Genre: Journal Article

Files

show Files
hide Files
:
Habermann.pdf (Publisher version), 6MB
 
File Permalink:
-
Name:
Habermann.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Molecular Genetics, Berlin; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
2012
Copyright Info:
by the American Society for Microbiology.
License:
-

Locators

show

Creators

show
hide
 Creators:
Habermann, Karin1, Author              
Mirgorodskaya, Ekaterina1, Author
Gobom, Johan1, Author              
Lehmann, Verena1, Author
Müller, Hannah1, Author
Blümlein, Katharina1, Author              
Deery, Michael J.2, Author
Czogiel, Irina3, Author              
Erdmann, Christoph4, Author
Ralser, Markus1, Author              
von Kries, Jens Peter 4, Author
Lange, Bodo M. H.1, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, Ihnestr. 63-74, Berlin, Germany, ou_1433550              
2University of Cambridge, Department of Biochemistry and Cambridge Systems Biology Centre, Cambridge, Cambridge, United Kingdom, ou_persistent22              
3Evolutionary Genomics (Peter Arndt), Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society, Ihnestr. 63- Berlin, Germany, ou_1479638              
4Leibniz Institute for Molecular Pharmacology (FMP), Screening Unit , Berlin, Germany, ou_persistent22              

Content

show
hide
Free keywords: Animals CDC2 Protein Kinase/genetics/metabolism Casein Kinase II/genetics/metabolism *Cell Cycle Cell Line Centrosome/*metabolism Drosophila Proteins/genetics/*metabolism Drosophila melanogaster/*cytology/genetics/metabolism Membrane Proteins/analysis/*metabolism Nuclear Envelope/*metabolism Nuclear Proteins/analysis/*metabolism Phosphorylation Protein-Serine-Threonine Kinases/genetics/*metabolism RNA Interference
 Abstract: Phosphorylation is one of the key mechanisms that regulate centrosome biogenesis, spindle assembly, and cell cycle progression. However, little is known about centrosome-specific phosphorylation sites and their functional relevance. Here, we identified phosphoproteins of intact Drosophila melanogaster centrosomes and found previously unknown phosphorylation sites in known and unexpected centrosomal components. We functionally characterized phosphoproteins and integrated them into regulatory signaling networks with the 3 important mitotic kinases, cdc2, polo, and aur, as well as the kinase CkIIbeta. Using a combinatorial RNA interference (RNAi) strategy, we demonstrated novel functions for P granule, nuclear envelope (NE), and nuclear proteins in centrosome duplication, maturation, and separation. Peptide microarrays confirmed phosphorylation of identified residues by centrosome-associated kinases. For a subset of phosphoproteins, we identified previously unknown centrosome and/or spindle localization via expression of tagged fusion proteins in Drosophila SL2 cells. Among those was otefin (Ote), an NE protein that we found to localize to centrosomes. Furthermore, we provide evidence that it is phosphorylated in vitro at threonine 63 (T63) through Aurora-A kinase. We propose that phosphorylation of this site plays a dual role in controlling mitotic exit when phosphorylated while dephosphorylation promotes G(2)/M transition in Drosophila SL2 cells.

Details

show
hide
Language(s): eng - English
 Dates: 2012-07-022012
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1128/MCB.00814-12
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Molecular and Cellular Biology (Washington, DC)
  Other : Mol Cell Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: American Society for Microbiology (ASM)
Pages: - Volume / Issue: 32 (17) Sequence Number: - Start / End Page: 3554 - 3569 Identifier: ISSN: 0270-7306
CoNE: /journals/resource/954925502188