Polyanion binding proteins data for five cellular polyanionic samples
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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 (HS), and DNA) and approximately 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 which contain multiply 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 (PABPs) interact with a wide variety of polyanionic surfaces in cells in a functionally significant manner. Keywords: Protein-Protein, protein-polyanion Interaction
ORGANISM(S): Bos taurus Sus scrofa Homo sapiens
PROVIDER: GSE6354 | GEO | 2006/11/30
SECONDARY ACCESSION(S): PRJNA99647
REPOSITORIES: GEO
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