A Protein Complex Network of Drosophila melanogaster

By K. G. Guruharsha, Jean‐François Rual, B. Zhai, J. Mintseris, P. Vaidya, Namita Vaidya, Chapman N Beekman, Christina Y Wong, David Y Rhee, Odise Cenaj and 14 more. Cell, 2011

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SUMMARY Determining the composition of protein complexes is an essential step towards understanding the cell as an integrated system. Using co-affinity purification coupled to mass spectrometry analysis, we examined protein associations involving nearly five thousand individual, FLAG-HA epitope-tagged Drosophila proteins. Stringent analysis of these data, based on a novel statistical framework to define individual protein-protein interactions, led to the generation of a Drosophila Protein interaction Map (DPiM) encompassing 556 protein complexes. The high quality of DPiM and its usefulness as a paradigm for metazoan proteomes is apparent from the recovery of many known complexes, significant enrichment for shared functional attributes and validation in human cells. DPiM defines potential novel members for several important protein complexes and assigns functional links to 586 protein-coding genes lacking previous experimental annotation. DPiM represents, to our knowledge, the largest metazoan protein complex map and provides a valuable resource for analysis of protein complex evolution.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/74f07f66072800434d02c2a6190a16ad2381106f

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In Molecular Biology

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