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BH‐protocadherin‐c, a member of the cadherin superfamily, interacts with protein phosphatase 1 alpha through its intracellular domain
Author(s) -
Yoshida Kenichi,
Watanabe Manabu,
Kato Hiroyuki,
Dutta Anindya,
Sugano Sumio
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01309-5
Subject(s) - protocadherin , microbiology and biotechnology , complementary dna , phosphatase , biology , cadherin , gene isoform , cdna library , immunoprecipitation , glycogen phosphorylase , intracellular , biochemistry , gene , phosphorylation , enzyme , cell
Using a yeast two‐hybrid system, we isolated eight cDNA clones which interacted with BH‐protocadherin‐c (BH‐Pcdh‐c) from the human brain cDNA library. One clone encoded protein phosphatase type 1 isoform α (PP1α) and another two PP1α2. PP1α was co‐immunoprecipitated from the extract of a gastric adenocarcinoma cell line MKN‐28 with anti‐BH‐Pcdh‐c antibody. PP1α activity towards glycogen phosphorylase was inhibited by the intracellular domain of BH‐Pcdh‐c. Inhibition of the phosphatase required more than the minimal domain of BH‐Pcdh‐c which could associate with PP1α. In situ hybridization revealed that BH‐Pcdh‐c mRNA was predominantly expressed in cerebral cortex neurons in the adult mouse brain.