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Effect of Ca 2+ on Protein Kinase A‐Mediated Phosphorylation of a Specific Serine Residue in an Expressed Peptide Containing the Ca 2+ ‐Regulatory Domain of Scallop Muscle Na + /Ca 2+ Exchanger
Author(s) -
RYAN C.,
SHAW G.,
HARDWICKE P. M. D.
Publication year - 2007
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1387.038
Subject(s) - phosphorylation , serine , peptide , exon , chemistry , microbiology and biotechnology , residue (chemistry) , biochemistry , gene , biology
Sequencing of the scallop muscle Na + /Ca 2+ exchanger revealed three consensus sequences for phosphorylation by PK‐A in the large cytoplasmic loop (R 363 KLTG, R 379 RASV, and R 618 RGSV). Site‐directed mutagenesis of the expressed Glu 384 ‐Ser 713 segment of the f loop identified Ser 621 as a residue phosphorylated by PK‐A. The R 618 RGSV sequence is located at the junction of the mutually exclusive exon and exon 9, a site where many alternatively spliced variants of vertebrate NCX1 and NCX3 are generated. Phosphorylation of Ser 621 by PK‐A in the isolated Glu 384 ‐Ser 713 peptide was blocked under conditions where Ca 2+ was bound.