Use of mechanistic models to integrate and analyze multiple proteomic datasets.

ABSTRACT: Proteins in cell signaling networks tend to interact promiscuously through low-affinity interactions. Consequently, evaluating the physiological importance of mapped interactions can be difficult. Attempts to do so have tended to focus on single, measurable physicochemical factors, such as affinity or abundance. For example, interaction importance has been assessed on the basis of the relative affinities of binding partners for a protein of interest, such as a receptor. However, multiple factors can be expected to simultaneously influence the recruitment of proteins to a receptor (and the potential of these proteins to contribute to receptor signaling), including affinity, abundance, and competition, which is a network property. Here, we demonstrate that measurements of protein copy number

SUBMITTER: Stites EC 

PROVIDER: S-EPMC4390817 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature