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Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition
Centrins are a family of small, EF hand-containing proteins that are found in all eukaryotes and are often complexed with centrosome-related structures. Since their discovery, centrins have attracted increasing interest due to their multiple, diverse cellular functions. Centrins are similar to calmo...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8622359/ https://www.ncbi.nlm.nih.gov/pubmed/34830049 http://dx.doi.org/10.3390/ijms222212173 |
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author | Pedretti, Marco Bombardi, Luca Conter, Carolina Favretto, Filippo Dominici, Paola Astegno, Alessandra |
author_facet | Pedretti, Marco Bombardi, Luca Conter, Carolina Favretto, Filippo Dominici, Paola Astegno, Alessandra |
author_sort | Pedretti, Marco |
collection | PubMed |
description | Centrins are a family of small, EF hand-containing proteins that are found in all eukaryotes and are often complexed with centrosome-related structures. Since their discovery, centrins have attracted increasing interest due to their multiple, diverse cellular functions. Centrins are similar to calmodulin (CaM) in size, structure and domain organization, although in contrast to CaM, the majority of centrins possess at least one calcium (Ca(2+)) binding site that is non-functional, thus displaying large variance in Ca(2+) sensing abilities that could support their functional versatility. In this review, we summarize current knowledge on centrins from both biophysical and structural perspectives with an emphasis on centrin-target interactions. In-depth analysis of the Ca(2+) sensing properties of centrins and structures of centrins complexed with target proteins can provide useful insight into the mechanisms of the different functions of centrins and how these proteins contribute to the complexity of the Ca(2+) signaling cascade. Moreover, it can help to better understand the functional redundancy of centrin isoforms and centrin-binding proteins. |
format | Online Article Text |
id | pubmed-8622359 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86223592021-11-27 Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition Pedretti, Marco Bombardi, Luca Conter, Carolina Favretto, Filippo Dominici, Paola Astegno, Alessandra Int J Mol Sci Review Centrins are a family of small, EF hand-containing proteins that are found in all eukaryotes and are often complexed with centrosome-related structures. Since their discovery, centrins have attracted increasing interest due to their multiple, diverse cellular functions. Centrins are similar to calmodulin (CaM) in size, structure and domain organization, although in contrast to CaM, the majority of centrins possess at least one calcium (Ca(2+)) binding site that is non-functional, thus displaying large variance in Ca(2+) sensing abilities that could support their functional versatility. In this review, we summarize current knowledge on centrins from both biophysical and structural perspectives with an emphasis on centrin-target interactions. In-depth analysis of the Ca(2+) sensing properties of centrins and structures of centrins complexed with target proteins can provide useful insight into the mechanisms of the different functions of centrins and how these proteins contribute to the complexity of the Ca(2+) signaling cascade. Moreover, it can help to better understand the functional redundancy of centrin isoforms and centrin-binding proteins. MDPI 2021-11-10 /pmc/articles/PMC8622359/ /pubmed/34830049 http://dx.doi.org/10.3390/ijms222212173 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Pedretti, Marco Bombardi, Luca Conter, Carolina Favretto, Filippo Dominici, Paola Astegno, Alessandra Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title | Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title_full | Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title_fullStr | Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title_full_unstemmed | Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title_short | Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition |
title_sort | structural basis for the functional diversity of centrins: a focus on calcium sensing properties and target recognition |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8622359/ https://www.ncbi.nlm.nih.gov/pubmed/34830049 http://dx.doi.org/10.3390/ijms222212173 |
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