Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk

Terry Vik, John W. Ryder

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Rsk is a 90-kDa protein kinase that is activated by phosphorylation by MAP kinase at the end of a well established signaling cascade. Rsk has two conserved catalytic kinase domains. The amino terminal kinase domain is responsible for phosphorylation of exogenous substrates. The carboxyl terminal domain of rsk has a basal autophosphorylation activity which can be detected when recombinant protein is incubated with [γ-32P]ATP. The manner in which rsk activity is controlled by site specific phosphorylation is largely unknown. We show that rsk can autophosphorylate through an intermolecular mechanism. Autophosphorylation occurs primarily on serine 380, in a highly conserved region of rsk between its two kinase domains. That site of autophosphorylation is similar to sites found in other serine/threonine kinases, which are also regulated by phosphorylation at that corresponding site. The carboxyl terminal kinase domain of rsk becomes a potential candidate kinase involved in phosphorylating and regulating the activity of those other kinases through their conserved domains.

Original languageEnglish
Pages (from-to)398-402
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume235
Issue number2
DOIs
StatePublished - Jun 18 1997
Externally publishedYes

Fingerprint

Xenopus
Serine
Phosphotransferases
Phosphorylation
Protein-Serine-Threonine Kinases
Recombinant Proteins
Protein Kinases
Catalytic Domain
Adenosine Triphosphate
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk. / Vik, Terry; Ryder, John W.

In: Biochemical and Biophysical Research Communications, Vol. 235, No. 2, 18.06.1997, p. 398-402.

Research output: Contribution to journalArticle

@article{4416c09815404939a3d9717bfc71b71f,
title = "Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk",
abstract = "Rsk is a 90-kDa protein kinase that is activated by phosphorylation by MAP kinase at the end of a well established signaling cascade. Rsk has two conserved catalytic kinase domains. The amino terminal kinase domain is responsible for phosphorylation of exogenous substrates. The carboxyl terminal domain of rsk has a basal autophosphorylation activity which can be detected when recombinant protein is incubated with [γ-32P]ATP. The manner in which rsk activity is controlled by site specific phosphorylation is largely unknown. We show that rsk can autophosphorylate through an intermolecular mechanism. Autophosphorylation occurs primarily on serine 380, in a highly conserved region of rsk between its two kinase domains. That site of autophosphorylation is similar to sites found in other serine/threonine kinases, which are also regulated by phosphorylation at that corresponding site. The carboxyl terminal kinase domain of rsk becomes a potential candidate kinase involved in phosphorylating and regulating the activity of those other kinases through their conserved domains.",
author = "Terry Vik and Ryder, {John W.}",
year = "1997",
month = "6",
day = "18",
doi = "10.1006/bbrc.1997.6794",
language = "English",
volume = "235",
pages = "398--402",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk

AU - Vik, Terry

AU - Ryder, John W.

PY - 1997/6/18

Y1 - 1997/6/18

N2 - Rsk is a 90-kDa protein kinase that is activated by phosphorylation by MAP kinase at the end of a well established signaling cascade. Rsk has two conserved catalytic kinase domains. The amino terminal kinase domain is responsible for phosphorylation of exogenous substrates. The carboxyl terminal domain of rsk has a basal autophosphorylation activity which can be detected when recombinant protein is incubated with [γ-32P]ATP. The manner in which rsk activity is controlled by site specific phosphorylation is largely unknown. We show that rsk can autophosphorylate through an intermolecular mechanism. Autophosphorylation occurs primarily on serine 380, in a highly conserved region of rsk between its two kinase domains. That site of autophosphorylation is similar to sites found in other serine/threonine kinases, which are also regulated by phosphorylation at that corresponding site. The carboxyl terminal kinase domain of rsk becomes a potential candidate kinase involved in phosphorylating and regulating the activity of those other kinases through their conserved domains.

AB - Rsk is a 90-kDa protein kinase that is activated by phosphorylation by MAP kinase at the end of a well established signaling cascade. Rsk has two conserved catalytic kinase domains. The amino terminal kinase domain is responsible for phosphorylation of exogenous substrates. The carboxyl terminal domain of rsk has a basal autophosphorylation activity which can be detected when recombinant protein is incubated with [γ-32P]ATP. The manner in which rsk activity is controlled by site specific phosphorylation is largely unknown. We show that rsk can autophosphorylate through an intermolecular mechanism. Autophosphorylation occurs primarily on serine 380, in a highly conserved region of rsk between its two kinase domains. That site of autophosphorylation is similar to sites found in other serine/threonine kinases, which are also regulated by phosphorylation at that corresponding site. The carboxyl terminal kinase domain of rsk becomes a potential candidate kinase involved in phosphorylating and regulating the activity of those other kinases through their conserved domains.

UR - http://www.scopus.com/inward/record.url?scp=0031577164&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031577164&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1997.6794

DO - 10.1006/bbrc.1997.6794

M3 - Article

C2 - 9199205

AN - SCOPUS:0031577164

VL - 235

SP - 398

EP - 402

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -