Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.

TAB1 was defined as a regulatory subunit of the protein kinase TAK1, which functions upstream in the pathways activated by interleukin (IL)-1, tumor necrosis factor (TNF), toll-like receptors (TLRs) and stressors. However, TAB1 also functions in the p38 MAPK pathway downstream of TAK1. We identified...

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Autores principales:	Alexander Wolf, Knut Beuerlein, Christoph Eckart, Hendrik Weiser, Beate Dickkopf, Helmut Müller, Hiroaki Sakurai, Michael Kracht
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d23bd930059944bfbde9b60250c2422f
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spelling	oai:doaj.org-article:d23bd930059944bfbde9b60250c2422f2021-11-18T07:31:36ZIdentification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.1932-620310.1371/journal.pone.0029256https://doaj.org/article/d23bd930059944bfbde9b60250c2422f2011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22216226/?tool=EBIhttps://doaj.org/toc/1932-6203TAB1 was defined as a regulatory subunit of the protein kinase TAK1, which functions upstream in the pathways activated by interleukin (IL)-1, tumor necrosis factor (TNF), toll-like receptors (TLRs) and stressors. However, TAB1 also functions in the p38 MAPK pathway downstream of TAK1. We identified amino acids (aa) 452/453 and 456/457 of TAB1 as novel sites phosphorylated by TAK1 as well as by p38 MAPK in intact cells as well as in vitro. Serines 452/453 and 456/457 were phosphorylated upon phosphatase blockade by calyculin A, or in response to IL-1 or translational stressors such as anisomycin and sorbitol. Deletion or phospho-mimetic mutations of aa 452-457 of TAB1 retain TAB1 and p38 MAPK in the cytoplasm. The TAB1 mutant lacking aa 452-457 decreases TAB1-dependent phosphorylation of p38 MAPK. It also enhances TAB1-dependent CCL5 secretion in response to IL-1 and increases activity of a post-transcriptional reporter gene, which contains the CCL5 3' untranslated region. These data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression.Alexander WolfKnut BeuerleinChristoph EckartHendrik WeiserBeate DickkopfHelmut MüllerHiroaki SakuraiMichael KrachtPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 12, p e29256 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alexander Wolf Knut Beuerlein Christoph Eckart Hendrik Weiser Beate Dickkopf Helmut Müller Hiroaki Sakurai Michael Kracht Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
description	TAB1 was defined as a regulatory subunit of the protein kinase TAK1, which functions upstream in the pathways activated by interleukin (IL)-1, tumor necrosis factor (TNF), toll-like receptors (TLRs) and stressors. However, TAB1 also functions in the p38 MAPK pathway downstream of TAK1. We identified amino acids (aa) 452/453 and 456/457 of TAB1 as novel sites phosphorylated by TAK1 as well as by p38 MAPK in intact cells as well as in vitro. Serines 452/453 and 456/457 were phosphorylated upon phosphatase blockade by calyculin A, or in response to IL-1 or translational stressors such as anisomycin and sorbitol. Deletion or phospho-mimetic mutations of aa 452-457 of TAB1 retain TAB1 and p38 MAPK in the cytoplasm. The TAB1 mutant lacking aa 452-457 decreases TAB1-dependent phosphorylation of p38 MAPK. It also enhances TAB1-dependent CCL5 secretion in response to IL-1 and increases activity of a post-transcriptional reporter gene, which contains the CCL5 3' untranslated region. These data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression.
format	article
author	Alexander Wolf Knut Beuerlein Christoph Eckart Hendrik Weiser Beate Dickkopf Helmut Müller Hiroaki Sakurai Michael Kracht
author_facet	Alexander Wolf Knut Beuerlein Christoph Eckart Hendrik Weiser Beate Dickkopf Helmut Müller Hiroaki Sakurai Michael Kracht
author_sort	Alexander Wolf
title	Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
title_short	Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
title_full	Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
title_fullStr	Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
title_full_unstemmed	Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
title_sort	identification and functional characterization of novel phosphorylation sites in tak1-binding protein (tab) 1.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/d23bd930059944bfbde9b60250c2422f
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Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.

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