The activity of protein phosphatase 5 towards native clients is modulated by the middle-and C-terminal domains of Hsp90
V Haslbeck, JM Eckl, A Drazic, DA Rutz, OR Lorenz… - Scientific reports, 2015 - nature.com
Protein phosphatase 5 is involved in the regulation of kinases and transcription factors. The
dephosphorylation activity is modulated by the molecular chaperone Hsp90, which binds to
the TPR-domain of protein phosphatase 5. This interaction is dependent on the C-terminal
MEEVD motif of Hsp90. We show that C-terminal Hsp90 fragments differ in their regulation of
the phosphatase activity hinting to a more complex interaction. Also hydrodynamic
parameters from analytical ultracentrifugation and small-angle X-ray scattering data suggest …
dephosphorylation activity is modulated by the molecular chaperone Hsp90, which binds to
the TPR-domain of protein phosphatase 5. This interaction is dependent on the C-terminal
MEEVD motif of Hsp90. We show that C-terminal Hsp90 fragments differ in their regulation of
the phosphatase activity hinting to a more complex interaction. Also hydrodynamic
parameters from analytical ultracentrifugation and small-angle X-ray scattering data suggest …
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