Bern O, Hazan B, Nir U
Department of Life Sciences, Bar-Ilan University, Ramat Gan, Israel.
FEBS Lett. 1997 Feb 10;403(1):45-50. doi: 10.1016/s0014-5793(97)00028-8.
p94fer and p51ferT are two nuclear tyrosine kinases encoded by the FER locus in the mouse. While p94fer accumulates in somatic cells, p51ferT is found solely in meiotic spermatogenic cells. Ectopic expression of p94fer or p51ferT in CHO cells, led to tyrosine phosphorylation of cellular 66, 68 and 120 kDa proteins. A 120, 68 and 66 kDa phosphoproteins, coimmunoprecipitated with p94fer and p51ferT from extracts of transfected CHO cells. Subcellular fractionation analysis indicated that the 66 kDa tyrosine phosphorylated protein colocalizes with p51ferT 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.
p94fer和p51ferT是小鼠FER基因座编码的两种核酪氨酸激酶。虽然p94fer在体细胞中积累,但p51ferT仅在减数分裂的生精细胞中发现。在CHO细胞中异位表达p94fer或p51ferT会导致细胞中66、68和120 kDa蛋白质的酪氨酸磷酸化。一种120、68和66 kDa的磷蛋白,与转染的CHO细胞提取物中的p94fer和p51ferT共免疫沉淀。亚细胞分级分析表明,66 kDa的酪氨酸磷酸化蛋白在活跃生长的细胞中与p51ferT共定位于核周和核级分。然而,在生长停滞的细胞中,66 kDa的磷蛋白主要与染色质相关,而其在其他核区室中的水平显著降低。因此,66 kDa的磷蛋白可能介导FER蛋白的核功能并将其与细胞生长联系起来。