Fas-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction

B Guerra, B Boldyreff, O G Issinger

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2001-Dec
OriginalsprogEngelsk
TidsskriftInternational Journal of Oncology
Vol/bind19
Udgave nummer6
Sider (fra-til)1117-26
Antal sider9
ISSN1019-6439
StatusUdgivet - 2001

Fingeraftryk

Casein Kinase II
Apoptosis
Cell Line
Enzymes
Alanine
Serine
Salts
Mutation
DNA

Citer dette

@article{1918f900ba9611dc9626000ea68e967b,
title = "Fas-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction",
abstract = "We show here that in several different cell lines protein kinase CK2 and Fas-associated factor 1 (FAF1) exist together in a complex which is stable to high monovalent salt concentration. The CK2/FAF1 complex formation is significantly increased after induction of apoptosis with various DNA damaging agents. Interestingly this effect is only seen in cell lines with an embryonic origin and not when cells have entered a differentiated state. It is further shown that the CK2 specific phosphorylation sites in the FAF1 molecule, i.e. serines 289 and 291 influence this complex formation. Mutation of the CK2 phosphorylation sites in the FAF1 molecule to alanine leads to a 1.5 to 2.0-fold higher association between CK2 and FAF1. Since the CK2 activity did not increase concomitantly with the complex formation we conclude that the FAF1 becomes to the CK2 enzyme so that a normal enzyme catalysis does not take place anymore. Subcellular localization experiments involving CK2 subunits and FAF1 show a co-localization of both CK2 subunits and FAF1 in the peri-nuclear cytoplasm. The majority of CK2 subunits is found in the nucleus. FAF1 is also found in the nucleoli. The results obtained further support the view that protein kinase CK2 plays an important role in certain steps of apoptosis.",
keywords = "Adaptor Proteins, Signal Transducing, Animals, Antineoplastic Agents, Apoptosis, Carrier Proteins, Casein Kinase II, Cell Differentiation, Cisplatin, DNA Primers, DNA, Complementary, Electrophoresis, Polyacrylamide Gel, Fibroblast Growth Factor 2, Gene Expression, Humans, Mice, Mutation, Phosphorylation, Plasmids, Protein-Serine-Threonine Kinases, Transfection, Tumor Cells, Cultured",
author = "B Guerra and B Boldyreff and Issinger, {O G}",
year = "2001",
language = "English",
volume = "19",
pages = "1117--26",
journal = "International Journal of Oncology",
issn = "1019-6439",
publisher = "Spandidos Publications",
number = "6",

}

Fas-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction. / Guerra, B; Boldyreff, B; Issinger, O G.

I: International Journal of Oncology, Bind 19, Nr. 6, 2001, s. 1117-26.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Fas-associated factor 1 interacts with protein kinase CK2 in vivo upon apoptosis induction

AU - Guerra, B

AU - Boldyreff, B

AU - Issinger, O G

PY - 2001

Y1 - 2001

N2 - We show here that in several different cell lines protein kinase CK2 and Fas-associated factor 1 (FAF1) exist together in a complex which is stable to high monovalent salt concentration. The CK2/FAF1 complex formation is significantly increased after induction of apoptosis with various DNA damaging agents. Interestingly this effect is only seen in cell lines with an embryonic origin and not when cells have entered a differentiated state. It is further shown that the CK2 specific phosphorylation sites in the FAF1 molecule, i.e. serines 289 and 291 influence this complex formation. Mutation of the CK2 phosphorylation sites in the FAF1 molecule to alanine leads to a 1.5 to 2.0-fold higher association between CK2 and FAF1. Since the CK2 activity did not increase concomitantly with the complex formation we conclude that the FAF1 becomes to the CK2 enzyme so that a normal enzyme catalysis does not take place anymore. Subcellular localization experiments involving CK2 subunits and FAF1 show a co-localization of both CK2 subunits and FAF1 in the peri-nuclear cytoplasm. The majority of CK2 subunits is found in the nucleus. FAF1 is also found in the nucleoli. The results obtained further support the view that protein kinase CK2 plays an important role in certain steps of apoptosis.

AB - We show here that in several different cell lines protein kinase CK2 and Fas-associated factor 1 (FAF1) exist together in a complex which is stable to high monovalent salt concentration. The CK2/FAF1 complex formation is significantly increased after induction of apoptosis with various DNA damaging agents. Interestingly this effect is only seen in cell lines with an embryonic origin and not when cells have entered a differentiated state. It is further shown that the CK2 specific phosphorylation sites in the FAF1 molecule, i.e. serines 289 and 291 influence this complex formation. Mutation of the CK2 phosphorylation sites in the FAF1 molecule to alanine leads to a 1.5 to 2.0-fold higher association between CK2 and FAF1. Since the CK2 activity did not increase concomitantly with the complex formation we conclude that the FAF1 becomes to the CK2 enzyme so that a normal enzyme catalysis does not take place anymore. Subcellular localization experiments involving CK2 subunits and FAF1 show a co-localization of both CK2 subunits and FAF1 in the peri-nuclear cytoplasm. The majority of CK2 subunits is found in the nucleus. FAF1 is also found in the nucleoli. The results obtained further support the view that protein kinase CK2 plays an important role in certain steps of apoptosis.

KW - Adaptor Proteins, Signal Transducing

KW - Animals

KW - Antineoplastic Agents

KW - Apoptosis

KW - Carrier Proteins

KW - Casein Kinase II

KW - Cell Differentiation

KW - Cisplatin

KW - DNA Primers

KW - DNA, Complementary

KW - Electrophoresis, Polyacrylamide Gel

KW - Fibroblast Growth Factor 2

KW - Gene Expression

KW - Humans

KW - Mice

KW - Mutation

KW - Phosphorylation

KW - Plasmids

KW - Protein-Serine-Threonine Kinases

KW - Transfection

KW - Tumor Cells, Cultured

M3 - Journal article

VL - 19

SP - 1117

EP - 1126

JO - International Journal of Oncology

JF - International Journal of Oncology

SN - 1019-6439

IS - 6

ER -