Abstract
An analysis of hubs (proteins with many interactors) and non-hubs in the S. cerevisiae protein interaction network shows that hub proteins are enriched with multiple and repeated domains.
Highlights
Most proteins interact with only a few other proteins while a small number of proteins have many interaction partners
The hubs were further classified as static party hubs (PHs) or dynamic date hubs (DHs), where party hubs are believed to interact with most of their partners at the same time while date hubs interact with their partners at different times and/or locations
In the previous section we showed that date hubs have a larger proportion of long disordered regions compared to party hubs, which indicates that the disordered regions may be important for flexible binding
Summary
Most proteins interact with only a few other proteins while a small number of proteins (hubs) have many interaction partners. We have investigated what differentiates hubs from non-hubs and static hubs (party hubs) from dynamic hubs (date hubs) in the protein-protein interaction network of Saccharomyces cerevisiae. Physical interactions between proteins are fundamental to most biological processes, since proteins need to interact with other proteins to accomplish their functions. Knowledge about the interactions between proteins is crucial for understanding biological functions. The functions of many proteins are unknown and identification of the physical interactions in which these proteins participate is likely to give an indication of their function. In large-scale experiments, tandem-affinity purification (TAP) followed by mass spectrometry is a common technique for identifying protein complexes [1], while the yeast two hybrid method is used for identifying individual protein-protein interactions [2,3,4].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
