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Phosphorylation of the translational regulator, PHAS‐I, by protein kinase CK2
Author(s) -
Fadden Patrick,
Haystead Timothy A.J,
Lawrence John C
Publication year - 1998
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(98)01047-3
Subject(s) - phosphorylation , kinase , protein phosphorylation , protein kinase a , in vitro , phosphorylation cascade , chemistry , immunoprecipitation , regulator , microbiology and biotechnology , biochemistry , biology , gene
The primary site in PHAS‐I for phosphorylation by protein kinase CK2 in vitro was identified as Ser 111 . A relatively small amount of phosphorylation of Ser 99 was also detected, and mutating Ser 99 to Ala in PHAS‐I slightly decreased phosphorylation by CK2 in vitro. In contrast, mutating Ser 111 to Ala almost abolished phosphorylation, confirming Ser 111 as the preferred site for CK2. Phosphorylation of Ser 111 did not decrease binding of PHAS‐I to eIF4E, and results of peptide mapping experiments with PHAS‐I immunoprecipitated from 32 P‐labeled adipocytes indicated that Ser 111 was not phosphorylated in cells. These results support the conclusion that CK2 is not involved in the control of PHAS‐I.