Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für Herz- und Lungenforschung (W. G. Kerckhoff Institut)     Collection: Yearbook_2014     Display Documents



ID: 682158.0, MPI für Herz- und Lungenforschung (W. G. Kerckhoff Institut) / Yearbook_2014
HIPK2 kinase activity depends on cis-autophosphorylation of its activation loop
Authors:Saul, V. V.; de la Vega, L.; Milanovic, M.; Kruger, M.; Braun, T.; Fritz-Wolf, K.; Becker, K.; Schmitz, M. L.
Date of Publication (YYYY-MM-DD):2013-02
Journal Abbrev.:J Mol Cell Biol
Volume:5
Issue / Number:1
Start Page:27
End Page:38
Audience:Not Specified
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 (homeodomain-interacting protein kinase 2) 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 dual-specificity tyrosine-phosphorylated and regulated 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.
External Publication Status:published
Document Type:Article
Communicated by:Svea Hümmer
Affiliations:MPI für physiologische und klinische Forschung
Identifiers:ISSN:1759-4685 (Electronic) 1759-4685 (Linking) %R 10.1093/jmcb/mjs053
URL:http://www.ncbi.nlm.nih.gov/pubmed/23000554
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.