The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization

Coronins play critical roles in actin network formation. The diverse functions of coronins are regulated by the structured N-terminal β propeller and the C-terminal coiled coil (CC). However, less is known about a middle "unique region" (UR), which is an intrinsically disordered region (ID...

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Main Authors: Han, Xiao, Hu, Zixin, Surya, Wahyu, Ma, Qianqian, Zhou, Feng, Nordenskiöld, Lars, Torres, Jaume, Lu, Lanyuan, Miao, Yansong
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2023
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Online Access:https://hdl.handle.net/10356/169271
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Institution: Nanyang Technological University
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spelling sg-ntu-dr.10356-1692712023-07-17T15:31:48Z The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization Han, Xiao Hu, Zixin Surya, Wahyu Ma, Qianqian Zhou, Feng Nordenskiöld, Lars Torres, Jaume Lu, Lanyuan Miao, Yansong School of Biological Sciences Institute for Digital Molecular Analytics and Science, NTU Science::Biological sciences Actin Cytoskeleton Coiled Coil Coronins play critical roles in actin network formation. The diverse functions of coronins are regulated by the structured N-terminal β propeller and the C-terminal coiled coil (CC). However, less is known about a middle "unique region" (UR), which is an intrinsically disordered region (IDR). The UR/IDR is an evolutionarily conserved signature in the coronin family. By integrating biochemical and cell biology experiments, coarse-grained simulations, and protein engineering, we find that the IDR optimizes the biochemical activities of coronins in vivo and in vitro. The budding yeast coronin IDR plays essential roles in regulating Crn1 activity by fine-tuning CC oligomerization and maintaining Crn1 as a tetramer. The IDR-guided optimization of Crn1 oligomerization is critical for F-actin cross-linking and regulation of Arp2/3-mediated actin polymerization. The final oligomerization status and homogeneity of Crn1 are contributed by three examined factors: helix packing, the energy landscape of the CC, and the length and molecular grammar of the IDR. Ministry of Education (MOE) Ministry of Health (MOH) National Medical Research Council (NMRC) National Research Foundation (NRF) Published version This study was supported by the Singapore Ministry of Education (MOE) Tier 3 (MOE2019-T3-1-012), MOE Tier 2 (MOE-T2EP30121-0015), and National Research Foundation Singapore under its Open Fund – Individual Research Grant (MOH-000955), and administered by the Singapore Ministry of Health’s National Medical Research Council, to Y.M.; MOE Tier 1 (2018-T1-001-096) to L.L.; MOE Tier 1 (RT13/19) to J.T; and MOE Tier 3 (MOE2019-T3-1-012) to L.N. 2023-07-11T00:58:30Z 2023-07-11T00:58:30Z 2023 Journal Article Han, X., Hu, Z., Surya, W., Ma, Q., Zhou, F., Nordenskiöld, L., Torres, J., Lu, L. & Miao, Y. (2023). The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization. Cell Reports, 42(6), 112594-. https://dx.doi.org/10.1016/j.celrep.2023.112594 2211-1247 https://hdl.handle.net/10356/169271 10.1016/j.celrep.2023.112594 37269287 2-s2.0-85160867539 6 42 112594 en MOE2019-T3-1-012 MOE-T2EP30121-0015 MOH-000955 2018-T1-001-096 RT13/19 Cell Reports © 2023 The Author(s). This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science::Biological sciences
Actin Cytoskeleton
Coiled Coil
spellingShingle Science::Biological sciences
Actin Cytoskeleton
Coiled Coil
Han, Xiao
Hu, Zixin
Surya, Wahyu
Ma, Qianqian
Zhou, Feng
Nordenskiöld, Lars
Torres, Jaume
Lu, Lanyuan
Miao, Yansong
The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
description Coronins play critical roles in actin network formation. The diverse functions of coronins are regulated by the structured N-terminal β propeller and the C-terminal coiled coil (CC). However, less is known about a middle "unique region" (UR), which is an intrinsically disordered region (IDR). The UR/IDR is an evolutionarily conserved signature in the coronin family. By integrating biochemical and cell biology experiments, coarse-grained simulations, and protein engineering, we find that the IDR optimizes the biochemical activities of coronins in vivo and in vitro. The budding yeast coronin IDR plays essential roles in regulating Crn1 activity by fine-tuning CC oligomerization and maintaining Crn1 as a tetramer. The IDR-guided optimization of Crn1 oligomerization is critical for F-actin cross-linking and regulation of Arp2/3-mediated actin polymerization. The final oligomerization status and homogeneity of Crn1 are contributed by three examined factors: helix packing, the energy landscape of the CC, and the length and molecular grammar of the IDR.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Han, Xiao
Hu, Zixin
Surya, Wahyu
Ma, Qianqian
Zhou, Feng
Nordenskiöld, Lars
Torres, Jaume
Lu, Lanyuan
Miao, Yansong
format Article
author Han, Xiao
Hu, Zixin
Surya, Wahyu
Ma, Qianqian
Zhou, Feng
Nordenskiöld, Lars
Torres, Jaume
Lu, Lanyuan
Miao, Yansong
author_sort Han, Xiao
title The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
title_short The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
title_full The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
title_fullStr The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
title_full_unstemmed The intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
title_sort intrinsically disordered region of coronins fine-tunes oligomerization and actin polymerization
publishDate 2023
url https://hdl.handle.net/10356/169271
_version_ 1773551223047192576