English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain : phosphorylation by DYRK1A and colocalization with splicing factors

de Graaf, K., Hekerman, P., Spelten, O., Herrmann, A., Packman, L. C., Buessow, K., et al. (2004). Characterization of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalization with splicing factors. Journal of Biological Chemistry, 279(6), 4612-4624. doi:10.1074/jbc.M310794200.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : J Biol Chem

Files

show Files

Locators

show

Creators

show
hide
 Creators:
de Graaf, Katrin, Author
Hekerman, Paul, Author
Spelten, Oliver, Author
Herrmann, Andreas, Author
Packman, Len C., Author
Buessow, Konrad1, Author           
Mueller-Newen, Gerhard, Author
Becker, Walter, Author
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              

Content

show
hide
Free keywords: -
 Abstract: A novel method employing filter arrays of a cDNA expression library for the identification of substrates for protein kinases was developed. With this technique, we identified a new member of the cyclin family, cyclin L2, as a substrate of the nuclear protein kinase DYRK1A. Cyclin L2 contains an N-terminal cyclin domain and a C-terminal arginine/serine-rich domain (RS domain), which is a hallmark of many proteins involved in pre-mRNA processing. The gene for cyclin L2 encodes the full-length cyclin L2, which is predominantly expressed in testis, as well as a truncated splicing variant (cyclin L2S) that lacks the RS domain and is ubiquitously expressed in human tissues. Full-length cyclin L2, but not cyclin L2S, was associated with the cyclin-dependent kinase PITSLRE. Cyclin L2 interacted with splicing factor 2 in vitro and was co-localized with the splicing factor SC35 in the nuclear speckle compartment. Photobleaching experiments showed that a fusion protein of green fluorescent protein and cyclin L2 in nuclear speckles rapidly exchanged with unbleached molecules in the nucleus, similar to other RS domain-containing proteins. In striking contrast, the closely related green fluorescent protein-cyclin L1 was immobile in the speckle compartment. DYRK1A interacted with cyclin L2 in pull-down assays, and overexpression of DYRK1A stimulated phosphorylation of cyclin L2 in COS-7 cells. These data characterize cyclin L2 as a highly mobile component of nuclear speckles and suggest that DYRK1A may regulate splicing by phosphorylation of cyclin L2.

Details

show
hide
Language(s): eng - English
 Dates: 2004-02-06
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 175482
DOI: 10.1074/jbc.M310794200
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Biological Chemistry
  Alternative Title : J Biol Chem
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 279 (6) Sequence Number: - Start / End Page: 4612 - 4624 Identifier: ISSN: 0021-9258