A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae

Actin nucleation is achieved by collaborative teamwork of actin nucleator factors (NFs) and nucleation-promoting factors (NPFs) into functional protein complexes. Selective inter- and intramolecular interactions between the nucleation complex constituents enable diverse modes of complex assembly in...

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Main Authors: Xie, Ying, Zhou, Feng, Ma, Qianqian, Lu, Lanyuan, Miao, Yansong
Other Authors: School of Biological Sciences
Format: Journal Article
Language:English
Published: 2022
Subjects:
Online Access:https://hdl.handle.net/10356/163105
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author Xie, Ying
Zhou, Feng
Ma, Qianqian
Lu, Lanyuan
Miao, Yansong
author2 School of Biological Sciences
author_facet School of Biological Sciences
Xie, Ying
Zhou, Feng
Ma, Qianqian
Lu, Lanyuan
Miao, Yansong
author_sort Xie, Ying
collection NTU
description Actin nucleation is achieved by collaborative teamwork of actin nucleator factors (NFs) and nucleation-promoting factors (NPFs) into functional protein complexes. Selective inter- and intramolecular interactions between the nucleation complex constituents enable diverse modes of complex assembly in initiating actin polymerization on demand. Budding yeast has two formins, Bni1 and Bnr1, which are teamed up with different NPFs. However, the selective pairing between formin NFs and NPFs into the nucleation core for actin polymerization is not completely understood. By examining the functions and interactions of NPFs and NFs via biochemistry, genetics, and mathematical modeling approaches, we found that two NPFs, Aip5 and Bud6, showed joint teamwork effort with Bni1 and Bnr1, respectively, by interacting with the C-terminal intrinsically disordered region (IDR) of formin, in which two NPFs work together to promote formin-mediated actin nucleation. Although the C-terminal IDRs of Bni1 and Bnr1 are distinct in length, each formin IDR orchestrates the recruitment of Bud6 and Aip5 cooperatively by different positioning strategies to form a functional complex. Our study demonstrated the dynamic assembly of the actin nucleation complex by recruiting multiple partners in budding yeast, which may be a general feature for effective actin nucleation by formins.
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spelling ntu-10356/1631052023-02-28T17:11:37Z A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae Xie, Ying Zhou, Feng Ma, Qianqian Lu, Lanyuan Miao, Yansong School of Biological Sciences Science::Biological sciences Actin Binding Protein BUD6 Protein Actin nucleation is achieved by collaborative teamwork of actin nucleator factors (NFs) and nucleation-promoting factors (NPFs) into functional protein complexes. Selective inter- and intramolecular interactions between the nucleation complex constituents enable diverse modes of complex assembly in initiating actin polymerization on demand. Budding yeast has two formins, Bni1 and Bnr1, which are teamed up with different NPFs. However, the selective pairing between formin NFs and NPFs into the nucleation core for actin polymerization is not completely understood. By examining the functions and interactions of NPFs and NFs via biochemistry, genetics, and mathematical modeling approaches, we found that two NPFs, Aip5 and Bud6, showed joint teamwork effort with Bni1 and Bnr1, respectively, by interacting with the C-terminal intrinsically disordered region (IDR) of formin, in which two NPFs work together to promote formin-mediated actin nucleation. Although the C-terminal IDRs of Bni1 and Bnr1 are distinct in length, each formin IDR orchestrates the recruitment of Bud6 and Aip5 cooperatively by different positioning strategies to form a functional complex. Our study demonstrated the dynamic assembly of the actin nucleation complex by recruiting multiple partners in budding yeast, which may be a general feature for effective actin nucleation by formins. Ministry of Education (MOE) Nanyang Technological University Skin Research Institute of Singapore (SRIS) Published version This study was supported by a NTU startup grant (M4081533), Skin Research Institute of Singapore (SRIS, SIG18002), and MOE Tier 2 (MOE2016-T2-1-005), MOE Tier 3 (MOE2019-T3-1-012) to Y.M., and MOE Tier 1 (2018-T1-001-096) to L.L. in Singapore. 2022-11-22T08:24:14Z 2022-11-22T08:24:14Z 2022 Journal Article Xie, Y., Zhou, F., Ma, Q., Lu, L. & Miao, Y. (2022). A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae. Molecular Biology of the Cell, 33(2), ar19-. https://dx.doi.org/10.1091/mbc.E21-06-0285 1939-4586 https://hdl.handle.net/10356/163105 10.1091/mbc.E21-06-0285 34818061 2-s2.0-85123878644 2 33 ar19 en M4081533 SRIS, SIG18002 MOE2016-T2-1-005 MOE2019-T3-1-012 2018-T1-001-096 Molecular Biology of the Cell © 2022 Xie et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial-Share Alike 4.0 International Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/4.0). application/pdf
spellingShingle Science::Biological sciences
Actin Binding Protein
BUD6 Protein
Xie, Ying
Zhou, Feng
Ma, Qianqian
Lu, Lanyuan
Miao, Yansong
A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title_full A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title_fullStr A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title_full_unstemmed A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title_short A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 in Saccharomyces cerevisiae
title_sort teamwork promotion of formin mediated actin nucleation by bud6 and aip5 in saccharomyces cerevisiae
topic Science::Biological sciences
Actin Binding Protein
BUD6 Protein
url https://hdl.handle.net/10356/163105
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