Combining affinity proteomics and network context to identify new phosphatase substrates and adapters in growth pathways.

ABSTRACT: Protein phosphorylation homoeostasis is tightly controlled and pathological conditions are caused by subtle alterations of the cell phosphorylation profile. Altered levels of kinase activities have already been associated to specific diseases. Less is known about the impact of phosphatases, the enzymes that down-regulate phosphorylation by removing the phosphate groups. This is partly due to our poor understanding of the phosphatase-substrate network. Much of phosphatase substrate specificity is not based on intrinsic enzyme specificity with the catalytic pocket recognizing the sequence/structure context of the phosphorylated residue. In addition many phosphatase catalytic subunits do not form a stable complex with their substrates. This makes the inference and validation of phosphatase su

SUBMITTER: Sacco F 

PROVIDER: S-EPMC4019850 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature