CPAP3 proteins in the mineralized cuticle of a decapod crustacean

Abstract The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPA...

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Autores principales:	Shai Abehsera, Shir Zaccai, Binyamin Mittelman, Lilah Glazer, Simy Weil, Isam Khalaila, Geula Davidov, Ronit Bitton, Raz Zarivach, Shihao Li, Fuhua Li, Jianhai Xiang, Rivka Manor, Eliahu D. Aflalo, Amir Sagi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9612dea2f0a5408eb45e0c09a2103e57
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spelling	oai:doaj.org-article:9612dea2f0a5408eb45e0c09a2103e572021-12-02T15:07:48ZCPAP3 proteins in the mineralized cuticle of a decapod crustacean10.1038/s41598-018-20835-x2045-2322https://doaj.org/article/9612dea2f0a5408eb45e0c09a2103e572018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-20835-xhttps://doaj.org/toc/2045-2322Abstract The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a family of cuticular proteins, first identified in the hexapod Drosophila melanogaster and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish Cherax quadricarinatus. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups.Shai AbehseraShir ZaccaiBinyamin MittelmanLilah GlazerSimy WeilIsam KhalailaGeula DavidovRonit BittonRaz ZarivachShihao LiFuhua LiJianhai XiangRivka ManorEliahu D. AflaloAmir SagiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shai Abehsera Shir Zaccai Binyamin Mittelman Lilah Glazer Simy Weil Isam Khalaila Geula Davidov Ronit Bitton Raz Zarivach Shihao Li Fuhua Li Jianhai Xiang Rivka Manor Eliahu D. Aflalo Amir Sagi CPAP3 proteins in the mineralized cuticle of a decapod crustacean
description	Abstract The pancrustacean theory groups crustaceans and hexapods (once thought to comprise separate clades within the Arthropoda) into a single clade. A key feature common to all pancrustaceans is their chitinous exoskeleton, with a major contribution by cuticular proteins. Among these, are the CPAP3’s, a family of cuticular proteins, first identified in the hexapod Drosophila melanogaster and characterized by an N-terminal signaling peptide and three chitin-binding domains. In this study, CPAP3 proteins were mined from a transcriptomic library of a decapod crustacean, the crayfish Cherax quadricarinatus. Phylogenetic analysis of other CPAP3 proteins from hexapods and other crustaceans showed a high degree of conservation. Characterization of the crayfish proteins, designated CqCPAP3’s, suggested a major role for CPAP3’sin cuticle formation. Loss-of-function experiments using RNAi supported such a notion by demonstrating crucial roles for several CqCPAP3 proteins during molting. A putative mode of action for the CqCPAP3 proteins –theoretically binding three chitin strands– was suggested by the structural data obtained from a representative recombinant CqCPAP3. The similarities between the CqCPAP3 proteins and their hexapod homologues further demonstrated common genetic and proteinaceous features of cuticle formation in pancrustaceans, thereby reinforcing the linkage between these two highly important phylogenetic groups.
format	article
author	Shai Abehsera Shir Zaccai Binyamin Mittelman Lilah Glazer Simy Weil Isam Khalaila Geula Davidov Ronit Bitton Raz Zarivach Shihao Li Fuhua Li Jianhai Xiang Rivka Manor Eliahu D. Aflalo Amir Sagi
author_facet	Shai Abehsera Shir Zaccai Binyamin Mittelman Lilah Glazer Simy Weil Isam Khalaila Geula Davidov Ronit Bitton Raz Zarivach Shihao Li Fuhua Li Jianhai Xiang Rivka Manor Eliahu D. Aflalo Amir Sagi
author_sort	Shai Abehsera
title	CPAP3 proteins in the mineralized cuticle of a decapod crustacean
title_short	CPAP3 proteins in the mineralized cuticle of a decapod crustacean
title_full	CPAP3 proteins in the mineralized cuticle of a decapod crustacean
title_fullStr	CPAP3 proteins in the mineralized cuticle of a decapod crustacean
title_full_unstemmed	CPAP3 proteins in the mineralized cuticle of a decapod crustacean
title_sort	cpap3 proteins in the mineralized cuticle of a decapod crustacean
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/9612dea2f0a5408eb45e0c09a2103e57
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CPAP3 proteins in the mineralized cuticle of a decapod crustacean

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