[HTML][HTML] Critical role of WW domain phosphorylation in regulating phosphoserine binding activity and Pin1 function
Phosphoserine-binding modules help determine the specificity of signal transduction events.
One such module, the group IV WW domain, plays an essential role in targeting the
phosphorylation-specific prolyl isomerase Pin1 to its substrates. These modules require
Ser/Thr phosphorylation of their ligands for binding activity. However, phosphorylation of
these modules and its functional significance have not been described, nor is it known
whether the function of Pin1 is regulated. Here we show that Pin1 WW domain is …
One such module, the group IV WW domain, plays an essential role in targeting the
phosphorylation-specific prolyl isomerase Pin1 to its substrates. These modules require
Ser/Thr phosphorylation of their ligands for binding activity. However, phosphorylation of
these modules and its functional significance have not been described, nor is it known
whether the function of Pin1 is regulated. Here we show that Pin1 WW domain is …