author_facet Coa, Larissa Leggieri
Abreu, Thiago Ferreira
Tashima, Alexandre Keiji
Green, Janaina
Pascon, Renata Castiglioni
Vallim, Marcelo Afonso
Machado-Jr, Joel
Coa, Larissa Leggieri
Abreu, Thiago Ferreira
Tashima, Alexandre Keiji
Green, Janaina
Pascon, Renata Castiglioni
Vallim, Marcelo Afonso
Machado-Jr, Joel
author Coa, Larissa Leggieri
Abreu, Thiago Ferreira
Tashima, Alexandre Keiji
Green, Janaina
Pascon, Renata Castiglioni
Vallim, Marcelo Afonso
Machado-Jr, Joel
spellingShingle Coa, Larissa Leggieri
Abreu, Thiago Ferreira
Tashima, Alexandre Keiji
Green, Janaina
Pascon, Renata Castiglioni
Vallim, Marcelo Afonso
Machado-Jr, Joel
Bioscience Reports
AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
Cell Biology
Molecular Biology
Biochemistry
Biophysics
author_sort coa, larissa leggieri
spelling Coa, Larissa Leggieri Abreu, Thiago Ferreira Tashima, Alexandre Keiji Green, Janaina Pascon, Renata Castiglioni Vallim, Marcelo Afonso Machado-Jr, Joel 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20181312 <jats:title>Abstract</jats:title> <jats:p>The serine-threonine kinase AKT/PKB is a critical regulator of various essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. Despite AKT action is known to function mainly in the cytoplasm, AKT has been reported to translocate to the nucleus. However, very little is known about the mechanism required for the nuclear import of AKT as well as its function in this cellular compartment. In the present study, we characterized the presence of endogenous nuclear AKT in human melanoma cells and addressed the possible role of AKT by exploring its potential association with key interaction nuclear partners. Confocal and Western blot analyses showed that both phosphorylated and non-phosphorylated forms of AKT are present in melanoma cells nuclei. Using mass spectrometry in combination with protein-crosslinking and co-immunoprecipitation, we identified a series of putative protein partners of nuclear AKT, including heterogeneous nuclear ribonucleoprotein (hnRNP), cytoskeleton proteins β-actin, γ-actin, β-actin-like 2 and vimentin. Confocal microscopy and biochemical analyses validated β-actin as a new nuclear AKT-interacting partner. Cofilin and active RNA Polymerase II, two proteins that have been described to interact and work in concert with nuclear actin in transcription regulation, were also found associated with nuclear AKT. Overall, the present study uncovered a yet unrecognized nuclear coupling of AKT and provides insights into the involvement of AKT in the interaction network of nuclear actin.</jats:p> AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells Bioscience Reports
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title AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_unstemmed AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_full AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_fullStr AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_full_unstemmed AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_short AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_sort akt/protein kinase b associates with β-actin in the nucleus of melanoma cells
topic Cell Biology
Molecular Biology
Biochemistry
Biophysics
url http://dx.doi.org/10.1042/bsr20181312
publishDate 2019
physical
description <jats:title>Abstract</jats:title> <jats:p>The serine-threonine kinase AKT/PKB is a critical regulator of various essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. Despite AKT action is known to function mainly in the cytoplasm, AKT has been reported to translocate to the nucleus. However, very little is known about the mechanism required for the nuclear import of AKT as well as its function in this cellular compartment. In the present study, we characterized the presence of endogenous nuclear AKT in human melanoma cells and addressed the possible role of AKT by exploring its potential association with key interaction nuclear partners. Confocal and Western blot analyses showed that both phosphorylated and non-phosphorylated forms of AKT are present in melanoma cells nuclei. Using mass spectrometry in combination with protein-crosslinking and co-immunoprecipitation, we identified a series of putative protein partners of nuclear AKT, including heterogeneous nuclear ribonucleoprotein (hnRNP), cytoskeleton proteins β-actin, γ-actin, β-actin-like 2 and vimentin. Confocal microscopy and biochemical analyses validated β-actin as a new nuclear AKT-interacting partner. Cofilin and active RNA Polymerase II, two proteins that have been described to interact and work in concert with nuclear actin in transcription regulation, were also found associated with nuclear AKT. Overall, the present study uncovered a yet unrecognized nuclear coupling of AKT and provides insights into the involvement of AKT in the interaction network of nuclear actin.</jats:p>
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author Coa, Larissa Leggieri, Abreu, Thiago Ferreira, Tashima, Alexandre Keiji, Green, Janaina, Pascon, Renata Castiglioni, Vallim, Marcelo Afonso, Machado-Jr, Joel
author_facet Coa, Larissa Leggieri, Abreu, Thiago Ferreira, Tashima, Alexandre Keiji, Green, Janaina, Pascon, Renata Castiglioni, Vallim, Marcelo Afonso, Machado-Jr, Joel, Coa, Larissa Leggieri, Abreu, Thiago Ferreira, Tashima, Alexandre Keiji, Green, Janaina, Pascon, Renata Castiglioni, Vallim, Marcelo Afonso, Machado-Jr, Joel
author_sort coa, larissa leggieri
container_issue 1
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container_title Bioscience Reports
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description <jats:title>Abstract</jats:title> <jats:p>The serine-threonine kinase AKT/PKB is a critical regulator of various essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. Despite AKT action is known to function mainly in the cytoplasm, AKT has been reported to translocate to the nucleus. However, very little is known about the mechanism required for the nuclear import of AKT as well as its function in this cellular compartment. In the present study, we characterized the presence of endogenous nuclear AKT in human melanoma cells and addressed the possible role of AKT by exploring its potential association with key interaction nuclear partners. Confocal and Western blot analyses showed that both phosphorylated and non-phosphorylated forms of AKT are present in melanoma cells nuclei. Using mass spectrometry in combination with protein-crosslinking and co-immunoprecipitation, we identified a series of putative protein partners of nuclear AKT, including heterogeneous nuclear ribonucleoprotein (hnRNP), cytoskeleton proteins β-actin, γ-actin, β-actin-like 2 and vimentin. Confocal microscopy and biochemical analyses validated β-actin as a new nuclear AKT-interacting partner. Cofilin and active RNA Polymerase II, two proteins that have been described to interact and work in concert with nuclear actin in transcription regulation, were also found associated with nuclear AKT. Overall, the present study uncovered a yet unrecognized nuclear coupling of AKT and provides insights into the involvement of AKT in the interaction network of nuclear actin.</jats:p>
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spelling Coa, Larissa Leggieri Abreu, Thiago Ferreira Tashima, Alexandre Keiji Green, Janaina Pascon, Renata Castiglioni Vallim, Marcelo Afonso Machado-Jr, Joel 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20181312 <jats:title>Abstract</jats:title> <jats:p>The serine-threonine kinase AKT/PKB is a critical regulator of various essential cellular processes, and dysregulation of AKT has been implicated in many diseases, including cancer. Despite AKT action is known to function mainly in the cytoplasm, AKT has been reported to translocate to the nucleus. However, very little is known about the mechanism required for the nuclear import of AKT as well as its function in this cellular compartment. In the present study, we characterized the presence of endogenous nuclear AKT in human melanoma cells and addressed the possible role of AKT by exploring its potential association with key interaction nuclear partners. Confocal and Western blot analyses showed that both phosphorylated and non-phosphorylated forms of AKT are present in melanoma cells nuclei. Using mass spectrometry in combination with protein-crosslinking and co-immunoprecipitation, we identified a series of putative protein partners of nuclear AKT, including heterogeneous nuclear ribonucleoprotein (hnRNP), cytoskeleton proteins β-actin, γ-actin, β-actin-like 2 and vimentin. Confocal microscopy and biochemical analyses validated β-actin as a new nuclear AKT-interacting partner. Cofilin and active RNA Polymerase II, two proteins that have been described to interact and work in concert with nuclear actin in transcription regulation, were also found associated with nuclear AKT. Overall, the present study uncovered a yet unrecognized nuclear coupling of AKT and provides insights into the involvement of AKT in the interaction network of nuclear actin.</jats:p> AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells Bioscience Reports
spellingShingle Coa, Larissa Leggieri, Abreu, Thiago Ferreira, Tashima, Alexandre Keiji, Green, Janaina, Pascon, Renata Castiglioni, Vallim, Marcelo Afonso, Machado-Jr, Joel, Bioscience Reports, AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells, Cell Biology, Molecular Biology, Biochemistry, Biophysics
title AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_full AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_fullStr AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_full_unstemmed AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_short AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
title_sort akt/protein kinase b associates with β-actin in the nucleus of melanoma cells
title_unstemmed AKT/protein kinase B associates with β-actin in the nucleus of melanoma cells
topic Cell Biology, Molecular Biology, Biochemistry, Biophysics
url http://dx.doi.org/10.1042/bsr20181312