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          Institute: MPI für medizinische Forschung     Collection: Jahbruch 2014_archival     Display Documents



ID: 681496.0, MPI für medizinische Forschung / Jahbruch 2014_archival
HIPK2 kinase activity depends on cis−autophosphorylation of its activation loop
Translation of Title:HIPK2 kinase activity depends on cis−autophosphorylation of its activation loop
Authors:Saul, Vera V.; de la Vega, Laureano; Milanovic, Maja; Krüger, Marcus; Braun, Thomas; Fritz−Wolf, Karin; Becker, Katja; Schmitz, M. Lienhard
Language:English
Date of Publication (YYYY-MM-DD):2013-02-01
Title of Journal:Journal of Molecular Cell Biology
Journal Abbrev.:Journal of Molecular Cell Biology
Volume:5
Issue / Number:1
Start Page:27
End Page:38
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
Free Keywords:protein kinase, HIPK2, autophosphorylation, gene expression, activation loop
External Publication Status:published
Document Type:Article
Communicated by:wkaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
Identifiers:LOCALID:7835
URI:http%3A%2F%2Fjmcb.oxfordjournals.org%2Fcontent%2Fe...
URI:http%3A%2F%2Fjmcb.oxfordjournals.org%2Fcgi%2Fpmidl...
URI:http%3A%2F%2Fjmcb.oxfordjournals.org%2Fcontent%2Fe...
DOI:10.1093%2Fjmcb%2Fmjs053
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