Growth-dependent subnuclear localization of a 66 kDa phosphoprotein in FER protein overexpressing cells

O. Bern; B. Hazan; U. Nir

doi:10.1016/S0014-5793(97)00028-8

Growth-dependent subnuclear localization of a 66 kDa phosphoprotein in FER protein overexpressing cells

O. Bern, B. Hazan, U. Nir

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

p94(fer) and p51(ferT) are two nuclear tyrosine kinases encoded by the FER locus in the mouse. While p94(fer) accumulates in somatic cells, p51(ferT) is found solely in meiotic spermatogenic cells. Ectopic expression of p94(fer) or p51(ferT) in CHO cells, led to tyrosine phosphorylation of cellular 66, 68 and 120 kDa proteins. A 120, 68 and 66 kDa phosphoproteins, coimmunoprecipitated with p94(fer) and p51(ferT) from extracts of transfected CHO cells. Subcellular fractionation analysis indicated that the 66 kDa tyrosine phosphorylated protein colocalizes with p51(ferT) to perinuclear and nuclear fractions in actively growing cells. However, in growth arrested cells, the 66 kDa phosphoprotein was associated mainly with chromatin while its level in the other nuclear compartments was significantly reduced. The 66 kDa phosphoprotein may thus mediate the nuclear function of the FER proteins and link it to cell growth.

Original language	English
Pages (from-to)	45-50
Number of pages	6
Journal	FEBS Letters
Volume	403
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(97)00028-8
State	Published - 10 Feb 1997

Bibliographical note

Funding Information:
We thank U. Caro for running the flow cytometry analysis, T. Pawson for supplying the fer cDNA and the E antiserum, M. Karin for supplying the pHS1 plasmid, N. Sonenberg and F. Lejbkowicz for supplying eIF-4A antibodies, R. Wides for his critical reading of the manuscript and S. Victor and A. Goldreich for typing the manuscript. This work was supported by grants from the United States-Israel Binational Foundation, the Council for Tobacco Research – USA, the Israel Cancer Research Fund and the Israel Academy of Sciences.

Funding

We thank U. Caro for running the flow cytometry analysis, T. Pawson for supplying the fer cDNA and the E antiserum, M. Karin for supplying the pHS1 plasmid, N. Sonenberg and F. Lejbkowicz for supplying eIF-4A antibodies, R. Wides for his critical reading of the manuscript and S. Victor and A. Goldreich for typing the manuscript. This work was supported by grants from the United States-Israel Binational Foundation, the Council for Tobacco Research – USA, the Israel Cancer Research Fund and the Israel Academy of Sciences.

Funders	Funder number
Council for Tobacco Research
Israel Cancer Research Fund
Academy of Leisure Sciences
United States-Israel Binational Science Foundation

Keywords

FER
Nuclear
Tyrosine kinase

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10.1016/S0014-5793(97)00028-8

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title = "Growth-dependent subnuclear localization of a 66 kDa phosphoprotein in FER protein overexpressing cells",

abstract = "p94(fer) and p51(ferT) are two nuclear tyrosine kinases encoded by the FER locus in the mouse. While p94(fer) accumulates in somatic cells, p51(ferT) is found solely in meiotic spermatogenic cells. Ectopic expression of p94(fer) or p51(ferT) in CHO cells, led to tyrosine phosphorylation of cellular 66, 68 and 120 kDa proteins. A 120, 68 and 66 kDa phosphoproteins, coimmunoprecipitated with p94(fer) and p51(ferT) from extracts of transfected CHO cells. Subcellular fractionation analysis indicated that the 66 kDa tyrosine phosphorylated protein colocalizes with p51(ferT) to perinuclear and nuclear fractions in actively growing cells. However, in growth arrested cells, the 66 kDa phosphoprotein was associated mainly with chromatin while its level in the other nuclear compartments was significantly reduced. The 66 kDa phosphoprotein may thus mediate the nuclear function of the FER proteins and link it to cell growth.",

keywords = "FER, Nuclear, Tyrosine kinase",

author = "O. Bern and B. Hazan and U. Nir",

note = "Funding Information: We thank U. Caro for running the flow cytometry analysis, T. Pawson for supplying the fer cDNA and the E antiserum, M. Karin for supplying the pHS1 plasmid, N. Sonenberg and F. Lejbkowicz for supplying eIF-4A antibodies, R. Wides for his critical reading of the manuscript and S. Victor and A. Goldreich for typing the manuscript. This work was supported by grants from the United States-Israel Binational Foundation, the Council for Tobacco Research – USA, the Israel Cancer Research Fund and the Israel Academy of Sciences.",

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N2 - p94(fer) and p51(ferT) are two nuclear tyrosine kinases encoded by the FER locus in the mouse. While p94(fer) accumulates in somatic cells, p51(ferT) is found solely in meiotic spermatogenic cells. Ectopic expression of p94(fer) or p51(ferT) in CHO cells, led to tyrosine phosphorylation of cellular 66, 68 and 120 kDa proteins. A 120, 68 and 66 kDa phosphoproteins, coimmunoprecipitated with p94(fer) and p51(ferT) from extracts of transfected CHO cells. Subcellular fractionation analysis indicated that the 66 kDa tyrosine phosphorylated protein colocalizes with p51(ferT) to perinuclear and nuclear fractions in actively growing cells. However, in growth arrested cells, the 66 kDa phosphoprotein was associated mainly with chromatin while its level in the other nuclear compartments was significantly reduced. The 66 kDa phosphoprotein may thus mediate the nuclear function of the FER proteins and link it to cell growth.

AB - p94(fer) and p51(ferT) are two nuclear tyrosine kinases encoded by the FER locus in the mouse. While p94(fer) accumulates in somatic cells, p51(ferT) is found solely in meiotic spermatogenic cells. Ectopic expression of p94(fer) or p51(ferT) in CHO cells, led to tyrosine phosphorylation of cellular 66, 68 and 120 kDa proteins. A 120, 68 and 66 kDa phosphoproteins, coimmunoprecipitated with p94(fer) and p51(ferT) from extracts of transfected CHO cells. Subcellular fractionation analysis indicated that the 66 kDa tyrosine phosphorylated protein colocalizes with p51(ferT) to perinuclear and nuclear fractions in actively growing cells. However, in growth arrested cells, the 66 kDa phosphoprotein was associated mainly with chromatin while its level in the other nuclear compartments was significantly reduced. The 66 kDa phosphoprotein may thus mediate the nuclear function of the FER proteins and link it to cell growth.

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KW - Tyrosine kinase

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Growth-dependent subnuclear localization of a 66 kDa phosphoprotein in FER protein overexpressing cells

Abstract

Bibliographical note

Funding

Keywords

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