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Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins
Reflectin proteins are natural copolymers consisting of repeated canonical domains. They are located in a biophotonic system called Bragg lamellae and manipulate the dynamic structural coloration of iridocytes. Their biological functions are intriguing, but the underlying mechanism is not fully unde...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9259870/ https://www.ncbi.nlm.nih.gov/pubmed/35813206 http://dx.doi.org/10.3389/fcell.2022.862011 |
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author | Song, Junyi Liu, Chuanyang Li, Baoshan Liu, Liangcheng Zeng, Ling Ye, Zonghuang Mao, Ting Wu, Wenjian Hu, Biru |
author_facet | Song, Junyi Liu, Chuanyang Li, Baoshan Liu, Liangcheng Zeng, Ling Ye, Zonghuang Mao, Ting Wu, Wenjian Hu, Biru |
author_sort | Song, Junyi |
collection | PubMed |
description | Reflectin proteins are natural copolymers consisting of repeated canonical domains. They are located in a biophotonic system called Bragg lamellae and manipulate the dynamic structural coloration of iridocytes. Their biological functions are intriguing, but the underlying mechanism is not fully understood. Reflectin A1, A2, B1, and C were found to present distinguished cyto-/nucleoplasmic localization preferences in the work. Comparable intracellular localization was reproduced by truncated reflectin variants, suggesting a conceivable evolutionary order among reflectin proteins. The size-dependent access of reflectin variants into the nucleus demonstrated a potential model of how reflectins get into Bragg lamellae. Moreover, RfA1 was found to extensively interact with the cytoskeleton, including its binding to actin and enrichment at the microtubule organizing center. This implied that the cytoskeleton system plays a fundamental role during the organization and transportation of reflectin proteins. The findings presented here provide evidence to get an in-depth insight into the evolutionary processes and working mechanisms of reflectins, as well as novel molecular tools to achieve tunable intracellular transportation. |
format | Online Article Text |
id | pubmed-9259870 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92598702022-07-08 Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins Song, Junyi Liu, Chuanyang Li, Baoshan Liu, Liangcheng Zeng, Ling Ye, Zonghuang Mao, Ting Wu, Wenjian Hu, Biru Front Cell Dev Biol Cell and Developmental Biology Reflectin proteins are natural copolymers consisting of repeated canonical domains. They are located in a biophotonic system called Bragg lamellae and manipulate the dynamic structural coloration of iridocytes. Their biological functions are intriguing, but the underlying mechanism is not fully understood. Reflectin A1, A2, B1, and C were found to present distinguished cyto-/nucleoplasmic localization preferences in the work. Comparable intracellular localization was reproduced by truncated reflectin variants, suggesting a conceivable evolutionary order among reflectin proteins. The size-dependent access of reflectin variants into the nucleus demonstrated a potential model of how reflectins get into Bragg lamellae. Moreover, RfA1 was found to extensively interact with the cytoskeleton, including its binding to actin and enrichment at the microtubule organizing center. This implied that the cytoskeleton system plays a fundamental role during the organization and transportation of reflectin proteins. The findings presented here provide evidence to get an in-depth insight into the evolutionary processes and working mechanisms of reflectins, as well as novel molecular tools to achieve tunable intracellular transportation. Frontiers Media S.A. 2022-06-23 /pmc/articles/PMC9259870/ /pubmed/35813206 http://dx.doi.org/10.3389/fcell.2022.862011 Text en Copyright © 2022 Song, Liu, Li, Liu, Zeng, Ye, Mao, Wu and Hu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Cell and Developmental Biology Song, Junyi Liu, Chuanyang Li, Baoshan Liu, Liangcheng Zeng, Ling Ye, Zonghuang Mao, Ting Wu, Wenjian Hu, Biru Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title | Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title_full | Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title_fullStr | Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title_full_unstemmed | Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title_short | Tunable Cellular Localization and Extensive Cytoskeleton-Interplay of Reflectins |
title_sort | tunable cellular localization and extensive cytoskeleton-interplay of reflectins |
topic | Cell and Developmental Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9259870/ https://www.ncbi.nlm.nih.gov/pubmed/35813206 http://dx.doi.org/10.3389/fcell.2022.862011 |
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