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Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast

Cell polarity and morphogenesis are regulated by the small GTPase Cdc42. Even though major advances have been done in the field during the last years, the molecular details leading to its activation in particular cellular contexts are not completely understood. In fission yeast, the β(1,3)-glucanase...

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Autores principales: García, Patricia, Coll, Pedro M., del Rey, Francisco, Geli, M. Isabel, Pérez, Pilar, Vázquez de Aldana, Carlos R., Encinar del Dedo, Javier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8429772/
https://www.ncbi.nlm.nih.gov/pubmed/34504165
http://dx.doi.org/10.1038/s41598-021-97311-6
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author García, Patricia
Coll, Pedro M.
del Rey, Francisco
Geli, M. Isabel
Pérez, Pilar
Vázquez de Aldana, Carlos R.
Encinar del Dedo, Javier
author_facet García, Patricia
Coll, Pedro M.
del Rey, Francisco
Geli, M. Isabel
Pérez, Pilar
Vázquez de Aldana, Carlos R.
Encinar del Dedo, Javier
author_sort García, Patricia
collection PubMed
description Cell polarity and morphogenesis are regulated by the small GTPase Cdc42. Even though major advances have been done in the field during the last years, the molecular details leading to its activation in particular cellular contexts are not completely understood. In fission yeast, the β(1,3)-glucanase Eng2 is a “moonlighting protein” with a dual function, acting as a hydrolase during spore dehiscence, and as component of the endocytic machinery in vegetative cells. Here, we report that Eng2 plays a role in Cdc42 activation during polarized growth through its interaction with the scaffold protein Scd2, which brings Cdc42 together with its guanine nucleotide exchange factor (GEF) Scd1. eng2Δ mutant cells have defects in activation of the bipolar growth (NETO), remaining monopolar during all the cell cycle. In the absence of Eng2 the accumulation of Scd1 and Scd2 at the poles is reduced, the levels of Cdc42 activation decrease, and the Cdc42 oscillatory behavior, associated with bipolar growth in wild type cells, is altered. Furthermore, overexpression of Eng2 partially rescues the growth and polarity defects of a cdc42-L160S mutant. Altogether, our work unveils a new factor regulating the activity of Cdc42, which could potentially link the polarity and endocytic machineries.
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spelling pubmed-84297722021-09-13 Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast García, Patricia Coll, Pedro M. del Rey, Francisco Geli, M. Isabel Pérez, Pilar Vázquez de Aldana, Carlos R. Encinar del Dedo, Javier Sci Rep Article Cell polarity and morphogenesis are regulated by the small GTPase Cdc42. Even though major advances have been done in the field during the last years, the molecular details leading to its activation in particular cellular contexts are not completely understood. In fission yeast, the β(1,3)-glucanase Eng2 is a “moonlighting protein” with a dual function, acting as a hydrolase during spore dehiscence, and as component of the endocytic machinery in vegetative cells. Here, we report that Eng2 plays a role in Cdc42 activation during polarized growth through its interaction with the scaffold protein Scd2, which brings Cdc42 together with its guanine nucleotide exchange factor (GEF) Scd1. eng2Δ mutant cells have defects in activation of the bipolar growth (NETO), remaining monopolar during all the cell cycle. In the absence of Eng2 the accumulation of Scd1 and Scd2 at the poles is reduced, the levels of Cdc42 activation decrease, and the Cdc42 oscillatory behavior, associated with bipolar growth in wild type cells, is altered. Furthermore, overexpression of Eng2 partially rescues the growth and polarity defects of a cdc42-L160S mutant. Altogether, our work unveils a new factor regulating the activity of Cdc42, which could potentially link the polarity and endocytic machineries. Nature Publishing Group UK 2021-09-09 /pmc/articles/PMC8429772/ /pubmed/34504165 http://dx.doi.org/10.1038/s41598-021-97311-6 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
García, Patricia
Coll, Pedro M.
del Rey, Francisco
Geli, M. Isabel
Pérez, Pilar
Vázquez de Aldana, Carlos R.
Encinar del Dedo, Javier
Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title_full Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title_fullStr Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title_full_unstemmed Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title_short Eng2, a new player involved in feedback loop regulation of Cdc42 activity in fission yeast
title_sort eng2, a new player involved in feedback loop regulation of cdc42 activity in fission yeast
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8429772/
https://www.ncbi.nlm.nih.gov/pubmed/34504165
http://dx.doi.org/10.1038/s41598-021-97311-6
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