Selecting protein tyrosine phosphatases as drug targets
Related Experiment Video
Updated: Sep 27, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
Published on: September 6, 2024
Rob Hooft van Huijsduijnen1, Agnes Bombrun, Dominique Swinnen
1Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan-les-Ouates, Geneva, Switzerland. rob.hooft@serono.com
Abstract:
Protein tyrosine phosphatases (PTPs) have emerged as a new and promising class of signaling targets, since the discovery of PTP1B as a major drug target for diabetes and obesity. Blocking individual PTPs results in the activation of specific tyrosine phosphorylation events, but matching PTPs with such pathways and therapeutic indications is a complex undertaking. The history of PTP1B shows that its unusual knockout phenotype and observations with generic and antisense inhibitors in vivo, but not its classical molecular biology, triggered the rapid development of inhibitors that are today being developed for the clinic.
Related Concept Videos
Transducer Mechanism: Enzyme-Linked Receptors
Major types that are helpful drug targets include:
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Pharmacogenomics: Identification of New Drug Targets
Amplifying Signals via Enzymatic Cascade
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase

