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Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors

The conserved ubiquitin-like protein Hub1/UBL5 functions in RNA splicing, DNA repair and mitochondrial unfolding responses. It binds proteins specific to these pathways and modifies their functional properties. However, the identities of other Hub1 substrates remain unknown. We have found unreported...

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Autores principales: Varikkapulakkal, Amjadudheen, Ghosh, Anuraag, Mishra, Shravan Kumar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8790634/
https://www.ncbi.nlm.nih.gov/pubmed/35098049
http://dx.doi.org/10.17912/micropub.biology.000519
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author Varikkapulakkal, Amjadudheen
Ghosh, Anuraag
Mishra, Shravan Kumar
author_facet Varikkapulakkal, Amjadudheen
Ghosh, Anuraag
Mishra, Shravan Kumar
author_sort Varikkapulakkal, Amjadudheen
collection PubMed
description The conserved ubiquitin-like protein Hub1/UBL5 functions in RNA splicing, DNA repair and mitochondrial unfolding responses. It binds proteins specific to these pathways and modifies their functional properties. However, the identities of other Hub1 substrates remain unknown. We have found unreported interactors of Saccharomyces cerevisiae Hub1 from a yeast two-hybrid (Y2H) screen. Proteins containing SIMs (small ubiquitin-like modifier SUMO-interaction motifs) and ferulic acid decarboxylase Fdc1 are identified as potential Hub1 interactors. Further experiments are required to establish these interactions and their physiological relevance, nevertheless, data presented here point towards larger and intriguing roles of Hub1.
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spelling pubmed-87906342022-01-27 Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors Varikkapulakkal, Amjadudheen Ghosh, Anuraag Mishra, Shravan Kumar MicroPubl Biol New Finding The conserved ubiquitin-like protein Hub1/UBL5 functions in RNA splicing, DNA repair and mitochondrial unfolding responses. It binds proteins specific to these pathways and modifies their functional properties. However, the identities of other Hub1 substrates remain unknown. We have found unreported interactors of Saccharomyces cerevisiae Hub1 from a yeast two-hybrid (Y2H) screen. Proteins containing SIMs (small ubiquitin-like modifier SUMO-interaction motifs) and ferulic acid decarboxylase Fdc1 are identified as potential Hub1 interactors. Further experiments are required to establish these interactions and their physiological relevance, nevertheless, data presented here point towards larger and intriguing roles of Hub1. Caltech Library 2022-01-25 /pmc/articles/PMC8790634/ /pubmed/35098049 http://dx.doi.org/10.17912/micropub.biology.000519 Text en Copyright: © 2022 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle New Finding
Varikkapulakkal, Amjadudheen
Ghosh, Anuraag
Mishra, Shravan Kumar
Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title_full Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title_fullStr Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title_full_unstemmed Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title_short Broader roles of the ubiquitin-like protein Hub1 indicated by its yeast two-hybrid interactors
title_sort broader roles of the ubiquitin-like protein hub1 indicated by its yeast two-hybrid interactors
topic New Finding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8790634/
https://www.ncbi.nlm.nih.gov/pubmed/35098049
http://dx.doi.org/10.17912/micropub.biology.000519
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