Pseudophosphatases: methods of analysis and physiological functions.
Protein tyrosine phosphatases (PTPs) are key enzymes in the regulation of cellular homeostasis and signaling pathways. Strikingly, not all PTPs bear enzymatic activity. A considerable fraction of PTPs are enzymatically inactive and are known as pseudophosphatases. Despite the lack of activity they execute pivotal roles in development, cell biology and human disease. The present review is focused on the methods used to identify pseudophosphatases, their targets, and physiological roles. We present a strategy for detailed enzymatic analysis of inactive PTPs, regulation of inactive PTP domains and identification of binding partners. Furthermore, we provide a detailed overview of human pseudophosphatases and discuss their regulation of cellular processes and functions in human pathologies.
Department of Biochemistry and Goodman Cancer Research Centre, McGill University, 3655, Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada. Electronic address: dmitri.kharitidi@mail.mcgill.ca.
Dmitri
D
Kharitidi
Department of Biochemistry and Goodman Cancer Research Centre, McGill University, 3655, Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada. Electronic address: sanaz.manteghi@mail.mcgill.ca.
Sanaz
S
Manteghi
Department of Biochemistry and Goodman Cancer Research Centre, McGill University, 3655, Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada. Electronic address: arnim.pause@mcgill.ca.
Arnim
A
Pause
D001665:Binding Sites; D057075:Enzyme Assays; D006801:Humans; D017027:Protein Tyrosine Phosphatases / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D013379:Substrate Specificity
D017027:Protein Tyrosine Phosphatases
PTP; Phosphatase assays; Phosphotyrosine binding domain; Pseudophosphatase; Substrate-trapping