Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Quick Search
My eDoc
Session History
Support Wiki
Direct access to
document ID:

          Institute: MPI für biophysikalische Chemie     Collection: Abteilung Eichele     Display Documents

ID: 269137.0, MPI für biophysikalische Chemie / Abteilung Eichele
Scaffolding by ERK3 regulates MK5 in development.
Authors:Schumacher, S.; Laass, K.; Kant, S.; Shi, Y.; Visel, A.; Gruber, A. D.; Kotlyarov, A.; Gaestel, M.
Date of Publication (YYYY-MM-DD):2004-12-08
Title of Journal:EMBO Journal
Issue / Number:24
Start Page:4770
End Page:4779
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Extracellular-regulated kinase 3 (ERK3, MAPK6) is an atypical member of the ERKs, lacking the threonine and tyrosine residues in the activation loop, carrying a unique C-terminal extension and being mainly regulated by its own protein stability and/or by autophosphorylation. Here we show that ERK3 specifically interacts with the MAPK-activated protein kinase 5 (MK5 or PRAK) in vitro and in vivo. Expression of ERK3 in mammalian cells leads to nuclear-cytoplasmic translocation and activation of MK5 and to phosphorylation of both ERK3 and MK5. Remarkably, activation of MK5 is independent of ERK3 enzymatic activity, but depends on its own catalytic activity as well as on a region in the C-terminal extension of ERK3. In mouse embryonic development, mRNA expression patterns of ERK3 and MK5 suggest spatiotemporal coexpression of both kinases. Deletion of MK5 leads to strong reduction of ERK3 protein levels and embryonic lethality at about stage E11, where ERK3 expression in wild-type mice is maximum, indicating a role of this signalling module in development.
Free Keywords:Animals; Cell Line; Embryo/anatomy & histology/physiology; Embryonic Development/physiology; Enzyme Activation; Humans; In Situ Hybridization; Mice; Mice, Knockout; Mitogen-Activated Protein Kinase 6/genetics/metabolism; Protein Structure, Tertiary; Protein Transport/physiology; Protein-Serine-Threonine Kinases/genetics/metabolism; Recombinant Fusion Proteins/genetics/metabolism; Research Support, Non-U.S. Gov't; Signal Transduction/physiology; Two-Hybrid System Techniques
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Eichele
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.