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

被引：5

作者：

Bern, O ^{[1
]}

Hazan, B ^{[1
]}

Nir, U ^{[1
]}

机构：

[1] BAR ILAN UNIV,DEPT LIFE SCI,IL-52900 RAMAT GAN,ISRAEL

来源：

FEBS LETTERS | 1997年 / 403卷 / 01期

关键词：

FER; tyrosine kinase; nuclear;

D O I：

10.1016/S0014-5793(97)00028-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

p94(fer) and p51(ferT) are two nuclear tyrosine kinases encoded by the FER lotus 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 PER proteins and link it to cell growth. (C) 1997 Federation of European Biochemical Societies.

引用

页码：45 / 50

页数：6

共 26 条

[1] A CONSERVED DOMAIN REGULATES INTERACTIONS OF THE V-FPS PROTEIN-TYROSINE KINASE WITH THE HOST-CELL [J].