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Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III
Activation of the Aspergillus nidulans transcription factor PacC, which mediates ambient pH regulation of gene expression and is recruited to ESCRT-III by the Vps32-interacting scaffold PalA, involves its ambient pH-dependent C-terminal proteolysis. This reaction is almost certainly catalyzed by the...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
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American Society for Biochemistry and Molecular Biology
2009
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2640967/ https://www.ncbi.nlm.nih.gov/pubmed/19056728 http://dx.doi.org/10.1074/jbc.M808645200 |
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author | Rodríguez-Galán, Olga Galindo, Antonio Hervás-Aguilar, América Arst, Herbert N. Peñalva, Miguel A. |
author_facet | Rodríguez-Galán, Olga Galindo, Antonio Hervás-Aguilar, América Arst, Herbert N. Peñalva, Miguel A. |
author_sort | Rodríguez-Galán, Olga |
collection | PubMed |
description | Activation of the Aspergillus nidulans transcription factor PacC, which mediates ambient pH regulation of gene expression and is recruited to ESCRT-III by the Vps32-interacting scaffold PalA, involves its ambient pH-dependent C-terminal proteolysis. This reaction is almost certainly catalyzed by the PalB calpain-like protease. Here we show that PalB associates with membranes and interacts specifically and directly with ESCRT-III Vps24. The PalB N-terminal MIT domain and the Vps24 C-terminal MIM motif are necessary and sufficient for this interaction. PalB(ΔMIT), a mutant PalB lacking the MIT domain is inefficiently recruited to membranes and impaired in PacC proteolytic processing. Notably, membrane recruitment is promoted and PacC processing largely restored by covalent attachment of Vps24 to mutant PalB(ΔMIT). This is the first reported evidence that calpain-like recruitment to ESCRT-III lattices plays a physiological role. It unambiguously positions the calpain-like protease PalB within the ESCRT-III-associated pH signaling complex, underlines the positive role of ESCRT-III in ambient pH signal transduction, and suggests a possible mechanism for PalB activation. |
format | Text |
id | pubmed-2640967 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-26409672009-02-23 Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III Rodríguez-Galán, Olga Galindo, Antonio Hervás-Aguilar, América Arst, Herbert N. Peñalva, Miguel A. J Biol Chem Mechanisms of Signal Transduction Activation of the Aspergillus nidulans transcription factor PacC, which mediates ambient pH regulation of gene expression and is recruited to ESCRT-III by the Vps32-interacting scaffold PalA, involves its ambient pH-dependent C-terminal proteolysis. This reaction is almost certainly catalyzed by the PalB calpain-like protease. Here we show that PalB associates with membranes and interacts specifically and directly with ESCRT-III Vps24. The PalB N-terminal MIT domain and the Vps24 C-terminal MIM motif are necessary and sufficient for this interaction. PalB(ΔMIT), a mutant PalB lacking the MIT domain is inefficiently recruited to membranes and impaired in PacC proteolytic processing. Notably, membrane recruitment is promoted and PacC processing largely restored by covalent attachment of Vps24 to mutant PalB(ΔMIT). This is the first reported evidence that calpain-like recruitment to ESCRT-III lattices plays a physiological role. It unambiguously positions the calpain-like protease PalB within the ESCRT-III-associated pH signaling complex, underlines the positive role of ESCRT-III in ambient pH signal transduction, and suggests a possible mechanism for PalB activation. American Society for Biochemistry and Molecular Biology 2009-02-13 /pmc/articles/PMC2640967/ /pubmed/19056728 http://dx.doi.org/10.1074/jbc.M808645200 Text en Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) applies to Author Choice Articles |
spellingShingle | Mechanisms of Signal Transduction Rodríguez-Galán, Olga Galindo, Antonio Hervás-Aguilar, América Arst, Herbert N. Peñalva, Miguel A. Physiological Involvement in pH Signaling of Vps24-mediated Recruitment of Aspergillus PalB Cysteine Protease to ESCRT-III |
title | Physiological Involvement in pH Signaling of Vps24-mediated Recruitment
of Aspergillus PalB Cysteine Protease to
ESCRT-III |
title_full | Physiological Involvement in pH Signaling of Vps24-mediated Recruitment
of Aspergillus PalB Cysteine Protease to
ESCRT-III |
title_fullStr | Physiological Involvement in pH Signaling of Vps24-mediated Recruitment
of Aspergillus PalB Cysteine Protease to
ESCRT-III |
title_full_unstemmed | Physiological Involvement in pH Signaling of Vps24-mediated Recruitment
of Aspergillus PalB Cysteine Protease to
ESCRT-III |
title_short | Physiological Involvement in pH Signaling of Vps24-mediated Recruitment
of Aspergillus PalB Cysteine Protease to
ESCRT-III |
title_sort | physiological involvement in ph signaling of vps24-mediated recruitment
of aspergillus palb cysteine protease to
escrt-iii |
topic | Mechanisms of Signal Transduction |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2640967/ https://www.ncbi.nlm.nih.gov/pubmed/19056728 http://dx.doi.org/10.1074/jbc.M808645200 |
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