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    Structural Disorder Provides Increased Adaptability for Vesicle Trafficking Pathways

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    Author
    Pietrosemoli, Natalia; Pancsa, Rita; Tompa, Peter
    Date
    2013
    Abstract
    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.
    Citation
    Pietrosemoli, Natalia, Pancsa, Rita and Tompa, Peter. "Structural Disorder Provides Increased Adaptability for Vesicle Trafficking Pathways." PLoS Computational Biology, 9, no. 7 (2013) Public Library of Science: e1003144. http://dx.doi.org/10.1371/journal.pcbi.1003144.
    Published Version
    http://dx.doi.org/10.1371/journal.pcbi.1003144
    Type
    Journal article
    Publisher
    Public Library of Science
    Citable link to this page
    https://hdl.handle.net/1911/71777
    Rights
    This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
    Link to License
    https://creativecommons.org/licenses/by/4.0/
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    • Bioengineering Publications [684]
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    Home | FAQ | Contact Us | Privacy Notice | Accessibility Statement
    Managed by the Digital Scholarship Services at Fondren Library, Rice University
    Physical Address: 6100 Main Street, Houston, Texas 77005
    Mailing Address: MS-44, P.O.BOX 1892, Houston, Texas 77251-1892
    Site Map