Paper Info
Title
Structural disorder provides increased adaptability for vesicle trafficking pathways.
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 (similar to 23%) than the other two, COPI (similar to 9%) and COPII (similar to 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.
Year
DOI
Venue
2013
10.1371/journal.pcbi.1003144
PLOS COMPUTATIONAL BIOLOGY
Keywords
Field
DocType
organelles,protein transport
Clathrin adaptor proteins,Protein domain,Biology,Cell biology,Golgi apparatus,COPI,Clathrin,Vesicle,Protein structure,COPII
Journal
Volume
Issue
ISSN
9
7
1553-734X
Citations 
PageRank 
References 
0
0.34
10
Authors
3
Name
Order
Citations
PageRank
Natalia Pietrosemoli100.34
Rita Pancsa2102.60
Peter Tompa326116.64