STRUCTURE OF LOW MOLECULAR WEIGHT TYROSINE PHOSPHATASES

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. PTPCaaX-1 (PRL-1) represents a novel class of phosphatase, which has been implicated in triggering metastasis of cancerous cells. Like all protein tyrosine phosphatases, these enzymes contain the conserved active site motif (CX5R). Unique to these phosphatases is a nuclear localization sequence and the C-terminal CaaX box motif required for farnesylation. Sequence comparisons show the PRL proteins to be most similar to cdc14 and PTEN, sharing approximately 25% identity with each. However, this similarity is limited to a region of approximately 70 residues surrounding the active site, suggesting that the PRL enzymes constitute a new family of phosphatase. To date no structural information is available for any member of the PRL family. The detailed information obtained from a high-resolution, solution-state structure could ultimately prove valuable in breaking the link between overexpression of these enzymes and metastasis.