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  HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop

Saul, V. V., de la Vega, L., Milanovic, M., Krüger, M., Braun, T., Fritz-Wolf, K., et al. (2013). HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop. Journal of molecular cell biology, 5(1), 27-38. doi:10.1093/jmcb/mjs053.

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Genre: Journal Article
Alternative Title : HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop

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JMolCellBiol_5_2013_27.pdf (Any fulltext), 632KB
 
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http://dx.doi.org/10.1093/jmcb/mjs053 (Any fulltext)
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 Creators:
Saul, Vera V., Author
de la Vega, Laureano, Author
Milanovic, Maja, Author
Krüger, Marcus, Author
Braun, Thomas, Author
Fritz-Wolf, Karin1, Author              
Becker, Katja, Author
Schmitz, M. Lienhard, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, Jahnstrasse 29, 69120 Heidelberg, DE, ou_1497700              

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Free keywords: protein kinase, HIPK2, autophosphorylation, gene expression, activation loop
 Abstract: The multitude of mechanisms regulating the activity of protein kinases includes phosphorylation of amino acids contained in the activation loop. Here we show that the serine/threonine kinase HIPK2 is heavily modified by autophosphorylation, which occurs by cis−autophosphorylation at the activation loop and by trans−autophosphorylation at other phosphorylation sites. Cis−autophosphorylation of HIPK2 at Y354 and S357 in the activation loop is essential for its kinase function and the binding to substrates and the interaction partner Pin1. HIPK2 activation loop phosphorylation is also required for its biological activity as a regulator of gene expression and cell proliferation. Phosphorylation of HIPK2 at Y354 alone is not sufficient for full HIPK2 activity, which is in marked contrast to some DYRK kinases where tyrosine phosphorylation is absolutely essential. This study shows that differential phosphorylation of HIPK2 provides a mechanism for controlling and specifying the signal output from this kinase

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Language(s): eng - English
 Dates: 2012-04-252012-08-222012-09-202013-02-01
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
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Title: Journal of molecular cell biology
  Other : JMCB
Source Genre: Journal
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Publ. Info: United States : Cary, NC : Oxford University Press
Pages: - Volume / Issue: 5 (1) Sequence Number: - Start / End Page: 27 - 38 Identifier: ISSN: 1759-4685