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  Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1

Kelm, O., Wind, M., Lehmann, W. D., & Nigg, E. A. (2002). Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1. Journal of Biological Chemistry, 277(28), 25247-25256.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Kelm, O.1, Author              
Wind, M.2, Author              
Lehmann, W. D., Author
Nigg, E. A.1, Author              
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
2External Organizations, ou_persistent22              

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 Abstract: Polo-like kinases (Plks) control multiple important events during M phase progression, but little is known about their activation during the cell cycle. The activities of both mammalian Plk1 and Xenopus Plx1 peak during M phase, and this activation has been attributed to phosphorylation. However, no phosphorylation sites have previously been identified in any member of the Plk family. Here we have combined tryptic phosphopeptide mapping with mass spectrometry to identify four major phosphorylation sites in Xenopus Plx1. All four sites appear to be phosphorylated in a cell cycle-dependent manner. Phosphorylations at two sites (Ser-260 and Ser-326) most likely represent autophosphorylation events, whereas two other sites (Thr-201 and Ser-340) are targeted by upstream kinases. Several recombinant kinases were tested for their ability to phosphorylate Plx1 in vitro. Whereas xPlkk1 phosphorylated primarily Thr-10, Thr-201 was readily phosphorylated by protein kinase A, and Cdk1/cyclin B was identified as a likely kinase acting on Ser-340. Phosphorylation of Ser-340 was shown to be responsible for the retarded electrophoretic mobility of Plx1 during M phase, and phosphorylation of Thr-201 was identified as a major activating event.

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Language(s): eng - English
 Dates: 2002-07-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41357
ISI: 000176747000053
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 277 (28) Sequence Number: - Start / End Page: 25247 - 25256 Identifier: ISSN: 0021-9258