Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export

The Drosophila HIFα homologue, Sima, is localized mainly in the cytoplasm in normoxia and accumulates in the nucleus upon hypoxic exposure. We have characterized the mechanism governing Sima oxygen-dependent subcellular localization and found that Sima shuttles continuously between the nucleus and t...

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Autores principales:	Irisarri, Maximiliano, Lavista Llanos, Sofía, Romero, Nuria Magdalena, Centanin, Lázaro, Dekanty, Andrés, Wappner, Pablo
Publicado:	2009
Materias:	Drosophila protein exportin 1 hypoxia inducible factor 1alpha oxygen Sima protein unclassified drug animal cell article cell hypoxia cell nucleus cellular distribution controlled study cytoplasm Drosophila hydroxylation nonhuman nuclear export signal nuclear import oxygen tension priority journal protein degradation protein domain protein localization protein transport Active Transport, Cell Nucleus Amino Acid Sequence Animals Animals, Genetically Modified DNA-Binding Proteins Drosophila melanogaster Drosophila Proteins Hypoxia-Inducible Factor 1, alpha Subunit Molecular Sequence Data Nuclear Export Signals Oxygen Procollagen-Proline Dioxygenase Recombinant Fusion Proteins Transgenes Von Hippel-Lindau Tumor Suppressor Protein
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10591524_v20_n17_p3878_Irisarri http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3878_Irisarri
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_10591524_v20_n17_p3878_Irisarri2023-06-08T16:03:23Z Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export Irisarri, Maximiliano Lavista Llanos, Sofía Romero, Nuria Magdalena Centanin, Lázaro Dekanty, Andrés Wappner, Pablo Drosophila protein exportin 1 hypoxia inducible factor 1alpha oxygen Sima protein unclassified drug animal cell article cell hypoxia cell nucleus cellular distribution controlled study cytoplasm Drosophila hydroxylation nonhuman nuclear export signal nuclear import oxygen tension priority journal protein degradation protein domain protein localization protein transport Active Transport, Cell Nucleus Amino Acid Sequence Animals Animals, Genetically Modified DNA-Binding Proteins Drosophila melanogaster Drosophila Proteins Hypoxia-Inducible Factor 1, alpha Subunit Molecular Sequence Data Nuclear Export Signals Oxygen Procollagen-Proline Dioxygenase Recombinant Fusion Proteins Transgenes Von Hippel-Lindau Tumor Suppressor Protein The Drosophila HIFα homologue, Sima, is localized mainly in the cytoplasm in normoxia and accumulates in the nucleus upon hypoxic exposure. We have characterized the mechanism governing Sima oxygen-dependent subcellular localization and found that Sima shuttles continuously between the nucleus and the cytoplasm. We have previously shown that nuclear import depends on an atypical bipartite nuclear localization signal mapping next to the C-terminus of the protein. We show here that nuclear export is mediated in part by a CRM1-dependent nuclear export signal localized in the oxygen-dependent degradation domain (ODDD). CRM1-dependent nuclear export requires both oxygen-dependent hydroxylation of a specific prolyl residue (Pro850) in the ODDD, and the activity of the von Hippel Lindau tumor suppressor factor. At high oxygen tension rapid nuclear export of Sima occurs, whereas in hypoxia, Sima nuclear export is largely inhibited. HIFα/Sima nucleo-cytoplasmic localization is the result of a dynamic equilibrium between nuclear import and nuclear export, and nuclear export is modulated by oxygen tension. © 2009 by The American Society for Cell Biology. Fil:Irisarri, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Lavista-Llanos, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Romero, N.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Centanin, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Dekanty, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wappner, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10591524_v20_n17_p3878_Irisarri http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3878_Irisarri
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Drosophila protein exportin 1 hypoxia inducible factor 1alpha oxygen Sima protein unclassified drug animal cell article cell hypoxia cell nucleus cellular distribution controlled study cytoplasm Drosophila hydroxylation nonhuman nuclear export signal nuclear import oxygen tension priority journal protein degradation protein domain protein localization protein transport Active Transport, Cell Nucleus Amino Acid Sequence Animals Animals, Genetically Modified DNA-Binding Proteins Drosophila melanogaster Drosophila Proteins Hypoxia-Inducible Factor 1, alpha Subunit Molecular Sequence Data Nuclear Export Signals Oxygen Procollagen-Proline Dioxygenase Recombinant Fusion Proteins Transgenes Von Hippel-Lindau Tumor Suppressor Protein
spellingShingle	Drosophila protein exportin 1 hypoxia inducible factor 1alpha oxygen Sima protein unclassified drug animal cell article cell hypoxia cell nucleus cellular distribution controlled study cytoplasm Drosophila hydroxylation nonhuman nuclear export signal nuclear import oxygen tension priority journal protein degradation protein domain protein localization protein transport Active Transport, Cell Nucleus Amino Acid Sequence Animals Animals, Genetically Modified DNA-Binding Proteins Drosophila melanogaster Drosophila Proteins Hypoxia-Inducible Factor 1, alpha Subunit Molecular Sequence Data Nuclear Export Signals Oxygen Procollagen-Proline Dioxygenase Recombinant Fusion Proteins Transgenes Von Hippel-Lindau Tumor Suppressor Protein Irisarri, Maximiliano Lavista Llanos, Sofía Romero, Nuria Magdalena Centanin, Lázaro Dekanty, Andrés Wappner, Pablo Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
topic_facet	Drosophila protein exportin 1 hypoxia inducible factor 1alpha oxygen Sima protein unclassified drug animal cell article cell hypoxia cell nucleus cellular distribution controlled study cytoplasm Drosophila hydroxylation nonhuman nuclear export signal nuclear import oxygen tension priority journal protein degradation protein domain protein localization protein transport Active Transport, Cell Nucleus Amino Acid Sequence Animals Animals, Genetically Modified DNA-Binding Proteins Drosophila melanogaster Drosophila Proteins Hypoxia-Inducible Factor 1, alpha Subunit Molecular Sequence Data Nuclear Export Signals Oxygen Procollagen-Proline Dioxygenase Recombinant Fusion Proteins Transgenes Von Hippel-Lindau Tumor Suppressor Protein
description	The Drosophila HIFα homologue, Sima, is localized mainly in the cytoplasm in normoxia and accumulates in the nucleus upon hypoxic exposure. We have characterized the mechanism governing Sima oxygen-dependent subcellular localization and found that Sima shuttles continuously between the nucleus and the cytoplasm. We have previously shown that nuclear import depends on an atypical bipartite nuclear localization signal mapping next to the C-terminus of the protein. We show here that nuclear export is mediated in part by a CRM1-dependent nuclear export signal localized in the oxygen-dependent degradation domain (ODDD). CRM1-dependent nuclear export requires both oxygen-dependent hydroxylation of a specific prolyl residue (Pro850) in the ODDD, and the activity of the von Hippel Lindau tumor suppressor factor. At high oxygen tension rapid nuclear export of Sima occurs, whereas in hypoxia, Sima nuclear export is largely inhibited. HIFα/Sima nucleo-cytoplasmic localization is the result of a dynamic equilibrium between nuclear import and nuclear export, and nuclear export is modulated by oxygen tension. © 2009 by The American Society for Cell Biology.
author	Irisarri, Maximiliano Lavista Llanos, Sofía Romero, Nuria Magdalena Centanin, Lázaro Dekanty, Andrés Wappner, Pablo
author_facet	Irisarri, Maximiliano Lavista Llanos, Sofía Romero, Nuria Magdalena Centanin, Lázaro Dekanty, Andrés Wappner, Pablo
author_sort	Irisarri, Maximiliano
title	Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
title_short	Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
title_full	Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
title_fullStr	Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
title_full_unstemmed	Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export
title_sort	central role of the oxygen-dependent degradation domain of drosophila hifα/sima in oxygen-dependent nuclear export
publishDate	2009
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10591524_v20_n17_p3878_Irisarri http://hdl.handle.net/20.500.12110/paper_10591524_v20_n17_p3878_Irisarri
work_keys_str_mv	AT irisarrimaximiliano centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport AT lavistallanossofia centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport AT romeronuriamagdalena centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport AT centaninlazaro centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport AT dekantyandres centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport AT wappnerpablo centralroleoftheoxygendependentdegradationdomainofdrosophilahifasimainoxygendependentnuclearexport
_version_	1768544049968447488

Central role of the oxygen-dependent degradation domain of Drosophila HIFα/Sima in oxygen-dependent nuclear export

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