A M Arnautov

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The present paper deals with two aspects of EGF-induced signal transduction via transcriptional factor STAT1. Utilizing vesicle fractionation in Percoll density gradient followed by co-immunoprecipitation, we observed the association of STAT1 with EGF receptor internalized in early endosomes. Co-immunoprecipitation studies with antikaryopherin alpha(More)
The influence of cytoskeleton-depolymerising agents (nocodazole and cytochalasine D) on EGF-induced transport of p42/p44MAPK into the cell nucleus was investigated. Using immunoblotting and immunofluorescence methods we have shown that depolymerization of microtubules does not affect EGF-induced nuclear import of MAPK, while actin depolymerization(More)
Transcription factor STAT1 (Signal Transducers and Activators of Transcription) takes part in signal transduction from receptors of growth factors and many cytokines, including interferons. In this paper, the role of tyrosinkinases Src and JAK2 was estimated in activation of STAT1 by epidermal growth factor (EGF) and hyperosmotic shock. Using a(More)
A study was made of an association of small GTPase Rab7, commonly considered as a marker of late endosomes, with endosomal compartments of cells expressing EGF receptor with different ability to be sorted for degradative pathway. It was found that in cells HER14, expressing normal EGF receptor, Rab7 was associated with both early and late endosomes and the(More)
Nuclear translocation of MAPK in cell lines, expressing normal and mutant forms of EGF-receptors (EGFR), was investigated. Using immunoblotting and immunofluorescence, EGF-induced MAPK transport was discovered in cell lines, expressing both normal receptor and one with deletion of major autophosphorylation sites. The dynamics of MAPK nuclear translocation(More)
During endocytosis EGF-receptor complexes are transported from early peripheral endosomes to late juxtranuclear-located endosomes to be then degraded in lysosomes. It is suggested that such a spatial organization of endosomal compartments is maintained by microtubule system and is necessary for lysosomal degradation of endocytosed cargo. In the present(More)
Intracellular distribution of p42/p44 MAP-kinases in HER14 and A431 cell lines was investigated. Using subcellular fractionation and immunofluorescence approaches we have shown that in quiescent cells of both types MAP-kinases are associated with endoplasmic reticulum. Moreover, ER-localized MAP-kinases were shown to exist only in a nonphosphorylated form.(More)
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