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Transcription factor phosphorylation by pp90(rsk2). Identification of Fos kinase and NGFI-B kinase I as pp90(rsk2)

Swanson, KD; Taylor, LK; Haung, L; Burlingame, AL; Landreth, GE; (1999) Transcription factor phosphorylation by pp90(rsk2). Identification of Fos kinase and NGFI-B kinase I as pp90(rsk2). Journal of Biological Chemistry , 274 (6) 3385 - 3395. Gold open access

Abstract

The in vitro phosphorylation of transcription factors by growth factor- activated protein kinases has resulted in the discovery of a number of activities whose identities and relationships to one another are unclear. Fos kinase is a growth factor-stimulated serine/threonine protein kinase that phosphorylates c-Fos at serine 362 within the carboxyl-terminal regulatory domain. Fos kinase activation is dependent on p21(ras) and mitogen-activated protein kinase/ERK kinase kinase (MEK) activity and is independent of phosphatidylinositol 3-kinase activity. We have purified Fos kinase by affinity chromatography using the Sepharose-linked protein kinase inhibitor, bisindolylmaleimide (BIM). Fos kinase has an apparent molecular mass of 88 kDa, and mass spectrophotometric analysis of the isolated protein showed that it produced tryptic fragments identical to those predicted for pp90(rsk2). Fos kinase isolated from nerve growth factor-stimulated PC12 cells is indistinguishable from NGFI-B kinase I, based on their chromatographic behavior, substrate specificities, and relative sensitivity to BIM. Furthermore, we have distinguished Fos kinase from calcium/cAMP response element-binding protein (CREB) kinase. Therefore, Fos kinase and NGFI-B kinase I and pp90(rsk2) represent the same protein kinase species. Moreover, we report that pp90(rsk2) exists within nerve growth factor-stimulated PC12 cells as two chromatographically and immunologically distinct species. Finally, we demonstrate that CREB kinase is distinct from pp90(rsk2)

Type:Article
Title:Transcription factor phosphorylation by pp90(rsk2). Identification of Fos kinase and NGFI-B kinase I as pp90(rsk2)
Open access status:An open access publication
Additional information:UI - 99121073 LA - Eng RN - EC 2.7.10.- (Ribosomal Protein S6 Kinase) RN - 0 (Transcription Factors) PT - JOURNAL ARTICLE ID -AG-00105/AG/NIA DA - 19990226 IS - 0021-9258 SB - M SB - X CY -UNITED STATES JC - HIV AA - Author EM - 199905
Keywords:Transcription Factors, Phosphorylation, Ribosomal Protein S6 Kinase, Proteins, Id, United States, Hiv, Amino Acid Sequence, analysis, Animal, cell, CELLS, Chromatography, In Vitro, isolation & purification, metabolism, Molecular Sequence Data, PC12 Cells, rats, Serine, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity, Support, U.S.Gov't, Non-P.H.S., Support, U.S.Gov't, P.H.S., Phosphatidylinositols, ANS, nerve
UCL classification:UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)

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