Phosphorylation of the translational regulator, PHAS-I, by protein kinase CK2.

Journal Article

The primary site in PHAS-I for phosphorylation by protein kinase CK2 in vitro was identified as Ser111. A relatively small amount of phosphorylation of Ser99 was also detected, and mutating Ser99 to Ala in PHAS-I slightly decreased phosphorylation by CK2 in vitro. In contrast, mutating Ser111 to Ala almost abolished phosphorylation, confirming Ser111 as the preferred site for CK2. Phosphorylation of Ser111 did not decrease binding of PHAS-I to eIF4E, and results of peptide mapping experiments with PHAS-I immunoprecipitated from 32P-labeled adipocytes indicated that Ser111 was not phosphorylated in cells. These results support the conclusion that CK2 is not involved in the control of PHAS-I.

Full Text

Duke Authors

Cited Authors

  • Fadden, P; Haystead, TA; Lawrence, JC

Published Date

  • September 11, 1998

Published In

Volume / Issue

  • 435 / 1

Start / End Page

  • 105 - 109

PubMed ID

  • 9755868

International Standard Serial Number (ISSN)

  • 0014-5793

Language

  • eng

Conference Location

  • England