Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.

MAK-V/Hunk is a scantily characterized AMPK-like protein kinase. Recent findings identified MAK-V as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of MAK-V action and regulation of its...

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Autores principales: Svetlana V Kalinichenko, Keiji Itoh, Elena V Korobko, Sergei Y Sokol, Vladimir L Buchman, Igor V Korobko
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Publicado: Public Library of Science (PLoS) 2012
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Acceso en línea:https://doaj.org/article/384c65e2d6b54befaad2724241647885
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spelling oai:doaj.org-article:384c65e2d6b54befaad27242416478852021-11-18T07:14:48ZIdentification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.1932-620310.1371/journal.pone.0039505https://doaj.org/article/384c65e2d6b54befaad27242416478852012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22745772/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203MAK-V/Hunk is a scantily characterized AMPK-like protein kinase. Recent findings identified MAK-V as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of MAK-V action and regulation of its activity remain largely unknown. We identified Nedd4 as an interaction partner for MAK-V protein kinase. However, this HECT-type E3 ubiquitin ligase is not involved in the control of MAK-V degradation by the ubiquitin-proteasome system that regulates MAK-V abundance in cells. However, Nedd4 in an ubiquitin ligase-independent manner rescued developmental defects in Xenopus embryos induced by MAK-V overexpression, suggesting physiological relevance of interaction between MAK-V and Nedd4. This identifies Nedd4 as the first known regulator of MAK-V function.Svetlana V KalinichenkoKeiji ItohElena V KorobkoSergei Y SokolVladimir L BuchmanIgor V KorobkoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 6, p e39505 (2012)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Svetlana V Kalinichenko
Keiji Itoh
Elena V Korobko
Sergei Y Sokol
Vladimir L Buchman
Igor V Korobko
Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
description MAK-V/Hunk is a scantily characterized AMPK-like protein kinase. Recent findings identified MAK-V as a pro-survival and anti-apoptotic protein and revealed its role in embryonic development as well as in tumorigenesis and metastasis. However molecular mechanisms of MAK-V action and regulation of its activity remain largely unknown. We identified Nedd4 as an interaction partner for MAK-V protein kinase. However, this HECT-type E3 ubiquitin ligase is not involved in the control of MAK-V degradation by the ubiquitin-proteasome system that regulates MAK-V abundance in cells. However, Nedd4 in an ubiquitin ligase-independent manner rescued developmental defects in Xenopus embryos induced by MAK-V overexpression, suggesting physiological relevance of interaction between MAK-V and Nedd4. This identifies Nedd4 as the first known regulator of MAK-V function.
format article
author Svetlana V Kalinichenko
Keiji Itoh
Elena V Korobko
Sergei Y Sokol
Vladimir L Buchman
Igor V Korobko
author_facet Svetlana V Kalinichenko
Keiji Itoh
Elena V Korobko
Sergei Y Sokol
Vladimir L Buchman
Igor V Korobko
author_sort Svetlana V Kalinichenko
title Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
title_short Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
title_full Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
title_fullStr Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
title_full_unstemmed Identification of Nedd4 E3 ubiquitin ligase as a binding partner and regulator of MAK-V protein kinase.
title_sort identification of nedd4 e3 ubiquitin ligase as a binding partner and regulator of mak-v protein kinase.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/384c65e2d6b54befaad2724241647885
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