[HTML][HTML] Modulation of ion transport by direct targeting of protein phosphatase type 1 to the Na-K-Cl cotransporter
RB Darman, A Flemmer, B Forbush - Journal of Biological Chemistry, 2001 - ASBMB
The specificity of major protein phosphatases is conferred via targeting subunits, each of
which binds specifically to the phosphatase and targets it to the vicinity of substrate proteins.
In the case of protein phosphatase 1 (PP1), an RVXFXD motif on a targeting subunit binds to
a cleft in PP1c, the catalytic subunit. Here we report that a substrate of PP1, the Na-K-Cl
cotransporter (NKCC1), bears this motif in its N terminus near sites of regulatory
phosphorylation and that direct binding of PP1 to NKCC1 is functionally important in …
which binds specifically to the phosphatase and targets it to the vicinity of substrate proteins.
In the case of protein phosphatase 1 (PP1), an RVXFXD motif on a targeting subunit binds to
a cleft in PP1c, the catalytic subunit. Here we report that a substrate of PP1, the Na-K-Cl
cotransporter (NKCC1), bears this motif in its N terminus near sites of regulatory
phosphorylation and that direct binding of PP1 to NKCC1 is functionally important in …