Interaction of Kinase-Interaction-Motif Protein Tyrosine Phosphatases with the Mitogen-Activated Protein Kinase ERK2Report as inadecuate




Interaction of Kinase-Interaction-Motif Protein Tyrosine Phosphatases with the Mitogen-Activated Protein Kinase ERK2 - Download this document for free, or read online. Document in PDF available to download.

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.



Author: Dana M. Francis , Dorothy Koveal , Antoni Tortajada, Rebecca Page, Wolfgang Peti

Source: http://plos.srce.hr/



DOWNLOAD PDF




Related documents