Structural disorder provides increased adaptability for vesicle trafficking pathways.

Vesicle trafficking systems play essential roles in the communication between the organelles of eukaryotic cells and also between cells and their environment. Endocytosis and the late secretory route are mediated by clathrin-coated vesicles, while the COat Protein I and II (COPI and COPII) routes st...

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Autores principales:	Natalia Pietrosemoli, Rita Pancsa, Peter Tompa
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/bd8f4c2ee4d64adc92bbe00116b45833
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spelling	oai:doaj.org-article:bd8f4c2ee4d64adc92bbe00116b458332021-11-18T05:51:59ZStructural disorder provides increased adaptability for vesicle trafficking pathways.1553-734X1553-735810.1371/journal.pcbi.1003144https://doaj.org/article/bd8f4c2ee4d64adc92bbe00116b458332013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23874186/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Vesicle trafficking systems play essential roles in the communication between the organelles of eukaryotic cells and also between cells and their environment. Endocytosis and the late secretory route are mediated by clathrin-coated vesicles, while the COat Protein I and II (COPI and COPII) routes stand for the bidirectional traffic between the ER and the Golgi apparatus. Despite similar fundamental organizations, the molecular machinery, functions, and evolutionary characteristics of the three systems are very different. In this work, we compiled the basic functional protein groups of the three main routes for human and yeast and analyzed them from the structural disorder perspective. We found similar overall disorder content in yeast and human proteins, confirming the well-conserved nature of these systems. Most functional groups contain highly disordered proteins, supporting the general importance of structural disorder in these routes, although some of them seem to heavily rely on disorder, while others do not. Interestingly, the clathrin system is significantly more disordered (~23%) than the other two, COPI (~9%) and COPII (~8%). We show that this structural phenomenon enhances the inherent plasticity and increased evolutionary adaptability of the clathrin system, which distinguishes it from the other two routes. Since multi-functionality (moonlighting) is indicative of both plasticity and adaptability, we studied its prevalence in vesicle trafficking proteins and correlated it with structural disorder. Clathrin adaptors have the highest capability for moonlighting while also comprising the most highly disordered members. The ability to acquire tissue specific functions was also used to approach adaptability: clathrin route genes have the most tissue specific exons encoding for protein segments enriched in structural disorder and interaction sites. Overall, our results confirm the general importance of structural disorder in vesicle trafficking and suggest major roles for this structural property in shaping the differences of evolutionary adaptability in the three routes.Natalia PietrosemoliRita PancsaPeter TompaPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 9, Iss 7, p e1003144 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Natalia Pietrosemoli Rita Pancsa Peter Tompa Structural disorder provides increased adaptability for vesicle trafficking pathways.
description	Vesicle trafficking systems play essential roles in the communication between the organelles of eukaryotic cells and also between cells and their environment. Endocytosis and the late secretory route are mediated by clathrin-coated vesicles, while the COat Protein I and II (COPI and COPII) routes stand for the bidirectional traffic between the ER and the Golgi apparatus. Despite similar fundamental organizations, the molecular machinery, functions, and evolutionary characteristics of the three systems are very different. In this work, we compiled the basic functional protein groups of the three main routes for human and yeast and analyzed them from the structural disorder perspective. We found similar overall disorder content in yeast and human proteins, confirming the well-conserved nature of these systems. Most functional groups contain highly disordered proteins, supporting the general importance of structural disorder in these routes, although some of them seem to heavily rely on disorder, while others do not. Interestingly, the clathrin system is significantly more disordered (~23%) than the other two, COPI (~9%) and COPII (~8%). We show that this structural phenomenon enhances the inherent plasticity and increased evolutionary adaptability of the clathrin system, which distinguishes it from the other two routes. Since multi-functionality (moonlighting) is indicative of both plasticity and adaptability, we studied its prevalence in vesicle trafficking proteins and correlated it with structural disorder. Clathrin adaptors have the highest capability for moonlighting while also comprising the most highly disordered members. The ability to acquire tissue specific functions was also used to approach adaptability: clathrin route genes have the most tissue specific exons encoding for protein segments enriched in structural disorder and interaction sites. Overall, our results confirm the general importance of structural disorder in vesicle trafficking and suggest major roles for this structural property in shaping the differences of evolutionary adaptability in the three routes.
format	article
author	Natalia Pietrosemoli Rita Pancsa Peter Tompa
author_facet	Natalia Pietrosemoli Rita Pancsa Peter Tompa
author_sort	Natalia Pietrosemoli
title	Structural disorder provides increased adaptability for vesicle trafficking pathways.
title_short	Structural disorder provides increased adaptability for vesicle trafficking pathways.
title_full	Structural disorder provides increased adaptability for vesicle trafficking pathways.
title_fullStr	Structural disorder provides increased adaptability for vesicle trafficking pathways.
title_full_unstemmed	Structural disorder provides increased adaptability for vesicle trafficking pathways.
title_sort	structural disorder provides increased adaptability for vesicle trafficking pathways.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/bd8f4c2ee4d64adc92bbe00116b45833
work_keys_str_mv	AT nataliapietrosemoli structuraldisorderprovidesincreasedadaptabilityforvesicletraffickingpathways AT ritapancsa structuraldisorderprovidesincreasedadaptabilityforvesicletraffickingpathways AT petertompa structuraldisorderprovidesincreasedadaptabilityforvesicletraffickingpathways
_version_	1718424752059580416

Structural disorder provides increased adaptability for vesicle trafficking pathways.

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