Phosphorylation of HIV-1 Rev protein: Implication of protein kinase CK2 and pro-directed kinases

Flavio Meggio, Donna M. D'Agostino, Vincenzo Ciminale, Luigi Chieco-Bianchi, Lorenzo A. Pinna

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

HIV-1 Rev transactivator is readily phosphorylated at separate regions by protein kinase CK2 and MAP kinase. Protein kinase CK1 cannot replace CK2 as phosphorylating agent and cdc2 only slowly phosphorylates Rev at one of the two sites affected by MAP kinase. Mutational analysis shows that Ser-8 and, to a lesser extent, Ser-5 are phosphorylated by CK2. In contrast, a mutation (R14TV → EED) which suppresses Rev activity dramatically enhances Rev phosphorylation either in vitro by CK2 or in vivo, suggesting that phosphorylation by CK2 could play a role in Rev down-regulation.

Original languageEnglish
Pages (from-to)547-554
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume226
Issue number2
DOIs
Publication statusPublished - Sep 13 1996

Fingerprint

Casein Kinase II
Phosphorylation
Phosphotransferases
Casein Kinase I
Trans-Activators
Mitogen-Activated Protein Kinase Kinases
Protein Kinases
HIV-1
Down-Regulation
Mutation
Human Immunodeficiency Virus-1 rev protein
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Phosphorylation of HIV-1 Rev protein : Implication of protein kinase CK2 and pro-directed kinases. / Meggio, Flavio; D'Agostino, Donna M.; Ciminale, Vincenzo; Chieco-Bianchi, Luigi; Pinna, Lorenzo A.

In: Biochemical and Biophysical Research Communications, Vol. 226, No. 2, 13.09.1996, p. 547-554.

Research output: Contribution to journalArticle

Meggio, Flavio ; D'Agostino, Donna M. ; Ciminale, Vincenzo ; Chieco-Bianchi, Luigi ; Pinna, Lorenzo A. / Phosphorylation of HIV-1 Rev protein : Implication of protein kinase CK2 and pro-directed kinases. In: Biochemical and Biophysical Research Communications. 1996 ; Vol. 226, No. 2. pp. 547-554.
@article{6b37764ed7674839b53a0133c8c73352,
title = "Phosphorylation of HIV-1 Rev protein: Implication of protein kinase CK2 and pro-directed kinases",
abstract = "HIV-1 Rev transactivator is readily phosphorylated at separate regions by protein kinase CK2 and MAP kinase. Protein kinase CK1 cannot replace CK2 as phosphorylating agent and cdc2 only slowly phosphorylates Rev at one of the two sites affected by MAP kinase. Mutational analysis shows that Ser-8 and, to a lesser extent, Ser-5 are phosphorylated by CK2. In contrast, a mutation (R14TV → EED) which suppresses Rev activity dramatically enhances Rev phosphorylation either in vitro by CK2 or in vivo, suggesting that phosphorylation by CK2 could play a role in Rev down-regulation.",
author = "Flavio Meggio and D'Agostino, {Donna M.} and Vincenzo Ciminale and Luigi Chieco-Bianchi and Pinna, {Lorenzo A.}",
year = "1996",
month = "9",
day = "13",
doi = "10.1006/bbrc.1996.1392",
language = "English",
volume = "226",
pages = "547--554",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Phosphorylation of HIV-1 Rev protein

T2 - Implication of protein kinase CK2 and pro-directed kinases

AU - Meggio, Flavio

AU - D'Agostino, Donna M.

AU - Ciminale, Vincenzo

AU - Chieco-Bianchi, Luigi

AU - Pinna, Lorenzo A.

PY - 1996/9/13

Y1 - 1996/9/13

N2 - HIV-1 Rev transactivator is readily phosphorylated at separate regions by protein kinase CK2 and MAP kinase. Protein kinase CK1 cannot replace CK2 as phosphorylating agent and cdc2 only slowly phosphorylates Rev at one of the two sites affected by MAP kinase. Mutational analysis shows that Ser-8 and, to a lesser extent, Ser-5 are phosphorylated by CK2. In contrast, a mutation (R14TV → EED) which suppresses Rev activity dramatically enhances Rev phosphorylation either in vitro by CK2 or in vivo, suggesting that phosphorylation by CK2 could play a role in Rev down-regulation.

AB - HIV-1 Rev transactivator is readily phosphorylated at separate regions by protein kinase CK2 and MAP kinase. Protein kinase CK1 cannot replace CK2 as phosphorylating agent and cdc2 only slowly phosphorylates Rev at one of the two sites affected by MAP kinase. Mutational analysis shows that Ser-8 and, to a lesser extent, Ser-5 are phosphorylated by CK2. In contrast, a mutation (R14TV → EED) which suppresses Rev activity dramatically enhances Rev phosphorylation either in vitro by CK2 or in vivo, suggesting that phosphorylation by CK2 could play a role in Rev down-regulation.

UR - http://www.scopus.com/inward/record.url?scp=0030582365&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030582365&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1996.1392

DO - 10.1006/bbrc.1996.1392

M3 - Article

C2 - 8806671

AN - SCOPUS:0030582365

VL - 226

SP - 547

EP - 554

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -