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...

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Autores principales: Marco Pedretti, Luca Bombardi, Carolina Conter, Filippo Favretto, Paola Dominici, Alessandra Astegno
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Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/5c6aa7a7013a4aa2bd96311c4d780603
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spelling oai:doaj.org-article:5c6aa7a7013a4aa2bd96311c4d7806032021-11-25T17:53:58ZStructural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition10.3390/ijms2222121731422-00671661-6596https://doaj.org/article/5c6aa7a7013a4aa2bd96311c4d7806032021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12173https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Centrins 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<sup>2+</sup>) binding site that is non-functional, thus displaying large variance in Ca<sup>2+</sup> 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<sup>2+</sup> 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<sup>2+</sup> signaling cascade. Moreover, it can help to better understand the functional redundancy of centrin isoforms and centrin-binding proteins.Marco PedrettiLuca BombardiCarolina ConterFilippo FavrettoPaola DominiciAlessandra AstegnoMDPI AGarticlecentrinEF-handcalcium signalingcalcium binding proteinprotein interactionBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12173, p 12173 (2021)
institution DOAJ
collection DOAJ
language EN
topic centrin
EF-hand
calcium signaling
calcium binding protein
protein interaction
Biology (General)
QH301-705.5
Chemistry
QD1-999
spellingShingle centrin
EF-hand
calcium signaling
calcium binding protein
protein interaction
Biology (General)
QH301-705.5
Chemistry
QD1-999
Marco Pedretti
Luca Bombardi
Carolina Conter
Filippo Favretto
Paola Dominici
Alessandra Astegno
Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition
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<sup>2+</sup>) binding site that is non-functional, thus displaying large variance in Ca<sup>2+</sup> 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<sup>2+</sup> 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<sup>2+</sup> signaling cascade. Moreover, it can help to better understand the functional redundancy of centrin isoforms and centrin-binding proteins.
format article
author Marco Pedretti
Luca Bombardi
Carolina Conter
Filippo Favretto
Paola Dominici
Alessandra Astegno
author_facet Marco Pedretti
Luca Bombardi
Carolina Conter
Filippo Favretto
Paola Dominici
Alessandra Astegno
author_sort Marco Pedretti
title 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_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_sort structural basis for the functional diversity of centrins: a focus on calcium sensing properties and target recognition
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/5c6aa7a7013a4aa2bd96311c4d780603
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AT lucabombardi structuralbasisforthefunctionaldiversityofcentrinsafocusoncalciumsensingpropertiesandtargetrecognition
AT carolinaconter structuralbasisforthefunctionaldiversityofcentrinsafocusoncalciumsensingpropertiesandtargetrecognition
AT filippofavretto structuralbasisforthefunctionaldiversityofcentrinsafocusoncalciumsensingpropertiesandtargetrecognition
AT paoladominici structuralbasisforthefunctionaldiversityofcentrinsafocusoncalciumsensingpropertiesandtargetrecognition
AT alessandraastegno structuralbasisforthefunctionaldiversityofcentrinsafocusoncalciumsensingpropertiesandtargetrecognition
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