Ontology highlight
ABSTRACT:
SUBMITTER: Lee KP
PROVIDER: S-EPMC5746516 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Lee Kyu Pil KP Kim Hyun Jin HJ Yang Dongki D
The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology 20171222 1
Protein phosphatase 1 (PP1) is involved in various signal transduction mechanisms as an extensive regulator. The PP1 catalytic subunit (PP1c) recognizes and binds to PP1-binding consensus residues (FxxR/KxR/K) in NBCe1-B. Consequently, we focused on identifying the function of the PP1-binding consensus residue, <sup>922</sup>FMDRLK<sup>927</sup>, in NBCe1-B. Using site-directed mutagenesis and co-immunoprecipitation assays, we revealed that in cases where the residues were substituted (F922A, R9 ...[more]