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Abstract:
The existence of interactions between many cellular proteins and various
polyanionic surfaces within a cell is now well established. The functional role
of such interactions, however, remains to be clearly defined. The existence of
protein arrays, with a large selection of different kinds of proteins, provides
a way to better address a number of aspects of this question. We have therefore
investigated the interaction between five cellular polyanions (actin, tubulin,
heparin, heparan sulfate, and DNA) and 5,000 human proteins using protein
microarrays in an attempt to better understand the functional nature of such
interaction(s). We demonstrate that a large number of polyanion-binding
proteins exist that contain multiple positively charged regions, are often
disordered, are involved in phosphorylation processes, and appear to play a
role in protein-protein interaction networks. Considering the crowded nature of
cellular interiors, we propose that polyanion-binding proteins interact with a
wide variety of polyanionic surfaces in cells in a functionally significant
manner.
