Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells

Ruk/CIN85 is a receptor-proximal ‘signalling’ adaptor that possesses three SH3 domains, Pro- and Ser-rich regions and C-terminal coiled-coil domain. It employs distinct domains and motifs to act as a transducer platform in intracellular signalling. Based on cDNA analysis, various isoforms of Ruk/CIN...

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Main Authors: B. O. Vynnytska-Myronovska, Ya. P. Bobak, G. V. Pasichnyk, N. I. Igumentseva, A. A. Samoylenko, L. B. Drobot
Format: Article
Language:English
Published: National Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine. 2014-10-01
Series:Ukrainian Biochemical Journal
Subjects:
Online Access:http://ukrbiochemjournal.org/wp-content/uploads/2015/06/Vynnytska-Myronovska_5_14.pdf
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spelling doaj-af6323f891314897b0ca2fe0e70483802020-11-25T00:30:05ZengNational Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine.Ukrainian Biochemical Journal2409-49432413-50032014-10-0186510211010.15407/ubj86.05.102Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cellsB. O. Vynnytska-Myronovska 0Ya. P. Bobak 1G. V. Pasichnyk2N. I. Igumentseva 3 A. A. Samoylenko4L. B. Drobot5Institute of Cell Biology, National Academy of Sciences of Ukraine, LvivInstitute of Cell Biology, National Academy of Sciences of Ukraine, LvivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivInstitute of Cell Biology, National Academy of Sciences of Ukraine, LvivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, KyivRuk/CIN85 is a receptor-proximal ‘signalling’ adaptor that possesses three SH3 domains, Pro- and Ser-rich regions and C-terminal coiled-coil domain. It employs distinct domains and motifs to act as a transducer platform in intracellular signalling. Based on cDNA analysis, various isoforms of Ruk/CIN85 with different combination of protein-protein interaction domains as well as additional Ruk/CIN85 forms that are the products of post-translational modifications have been demonstrated. Nevertheless, there is no precise information regarding both the subcellular distribution and the role of Ruk/CIN85 multiple molecular forms in cellular responses. Using MCF-7 human breast adenocarcinoma cells and cell fractionation technique, specific association of Ruk/CIN85 molecular forms with different subcellular compartments was demonstrated. Induction of apoptosis of MCF-7 cells by doxorubicin treatment or by serum deprivation resulted in the system changes of Ruk/CIN85 molecular forms intracellular localization as well as their ratio. The data obtained provide a new insight into potential physiological significance of Ruk/CIN85 molecular forms in the regulation of various cellular functions.http://ukrbiochemjournal.org/wp-content/uploads/2015/06/Vynnytska-Myronovska_5_14.pdfadaptor proteinsapoptosisMCF-7 cellsmultiple molecular formsRuk/CIN85subcellular distribution
collection DOAJ
language English
format Article
sources DOAJ
author B. O. Vynnytska-Myronovska
Ya. P. Bobak
G. V. Pasichnyk
N. I. Igumentseva
A. A. Samoylenko
L. B. Drobot
spellingShingle B. O. Vynnytska-Myronovska
Ya. P. Bobak
G. V. Pasichnyk
N. I. Igumentseva
A. A. Samoylenko
L. B. Drobot
Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
Ukrainian Biochemical Journal
adaptor proteins
apoptosis
MCF-7 cells
multiple molecular forms
Ruk/CIN85
subcellular distribution
author_facet B. O. Vynnytska-Myronovska
Ya. P. Bobak
G. V. Pasichnyk
N. I. Igumentseva
A. A. Samoylenko
L. B. Drobot
author_sort B. O. Vynnytska-Myronovska
title Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
title_short Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
title_full Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
title_fullStr Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
title_full_unstemmed Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma MCF-7 cells
title_sort multiple molecular forms of adaptor protein ruk/cin85 specifically associate with different subcellular compartments in human breast adenocarcinoma mcf-7 cells
publisher National Academy of Sciences of Ukraine and Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine.
series Ukrainian Biochemical Journal
issn 2409-4943
2413-5003
publishDate 2014-10-01
description Ruk/CIN85 is a receptor-proximal ‘signalling’ adaptor that possesses three SH3 domains, Pro- and Ser-rich regions and C-terminal coiled-coil domain. It employs distinct domains and motifs to act as a transducer platform in intracellular signalling. Based on cDNA analysis, various isoforms of Ruk/CIN85 with different combination of protein-protein interaction domains as well as additional Ruk/CIN85 forms that are the products of post-translational modifications have been demonstrated. Nevertheless, there is no precise information regarding both the subcellular distribution and the role of Ruk/CIN85 multiple molecular forms in cellular responses. Using MCF-7 human breast adenocarcinoma cells and cell fractionation technique, specific association of Ruk/CIN85 molecular forms with different subcellular compartments was demonstrated. Induction of apoptosis of MCF-7 cells by doxorubicin treatment or by serum deprivation resulted in the system changes of Ruk/CIN85 molecular forms intracellular localization as well as their ratio. The data obtained provide a new insight into potential physiological significance of Ruk/CIN85 molecular forms in the regulation of various cellular functions.
topic adaptor proteins
apoptosis
MCF-7 cells
multiple molecular forms
Ruk/CIN85
subcellular distribution
url http://ukrbiochemjournal.org/wp-content/uploads/2015/06/Vynnytska-Myronovska_5_14.pdf
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