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- Title
Interaction of Kinase-Interaction-Motif Protein Tyrosine Phosphatases with the Mitogen-Activated Protein Kinase ERK2.
- Authors
Francis, Dana M.; Koveal, Dorothy; Tortajada, Antoni; Page, Rebecca; Peti, Wolfgang
- Abstract
The mitogen-activation protein kinase ERK2 is tightly regulated by multiple phosphatases, including those of the kinase interaction motif (KIM) PTP family (STEP, PTPSL and HePTP). Here, we use small angle X-ray scattering (SAXS) and isothermal titration calorimetry (ITC) to show that the ERK2:STEP complex is compact and that residues outside the canonical KIM motif of STEP contribute to ERK2 binding. Furthermore, we analyzed the interaction of PTPSL with ERK2 showing that residues outside of the canonical KIM motif also contribute to ERK2 binding. The integration of this work with previous studies provides a quantitative and structural map of how the members of a single family of regulators, the KIM-PTPs, differentially interact with their corresponding MAPKs, ERK2 and p38α.
- Subjects
PROTEIN-protein interactions; PROTEIN-tyrosine kinases; PHOSPHOPROTEIN phosphatases; MITOGEN-activated protein kinases; ISOTHERMAL titration calorimetry; SMALL-angle X-ray scattering; RECOMBINANT proteins
- Publication
PLoS ONE, 2014, Vol 9, Issue 3, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0091934