Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85.
Tristetraprolin (TTP) is the prototype member of a family of CCCH tandem zinc finger proteins and is considered to be an anti-inflammatory protein in mammals. TTP plays a critical role in the decay of tumor necrosis factor alpha (TNF) mRNA, among others, by binding AU-rich RNA elements in the 3'...
Main Authors: | Vishram P Kedar, Martyn K Darby, Jason G Williams, Perry J Blackshear |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2010-03-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2833206?pdf=render |
Similar Items
-
Protein kinase D interacts with adaptor protein Ruk/CIN85 and phosphorylates it
by: Yu. A. Rzepetsky, et al.
Published: (2009-12-01) -
Functional regulation of tristetraprolin through protein phosphorylation and protein-protein interaction
by: Ya-Han Yu, et al.
Published: (2016) -
Complex of MUC1, CIN85 and Cbl in Colon Cancer Progression and Metastasis
by: Sandra Cascio, et al.
Published: (2015-02-01) -
Simulating EGFR-ERK signaling control by scaffold proteins KSR and MP1 reveals differential ligand-sensitivity co-regulated by Cbl-CIN85 and endophilin.
by: Lu Huang, et al.
Published: (2011-01-01) -
Simulating EGFR-ERK Signaling Control by Scaffold Proteins KSR and MP1 Reveals Differential Ligand-Sensitivity Co-Regulated by Cbl-CIN85 and Endophilin
by: Huang, Lu, et al.
Published: (2011)