PAG: a potential tumour suppressor and how it all started. From immune signalling to neoplastic transformation.
Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG) also known as Csk-binding protein was first fully characterized in 2000. It was initially recognized as a ubiquitously expressed adaptor protein recruiting cytoplasmic C-terminal Src-kinase to the close proximity of plasma membrane-anchored Src-kinases thereby allowing Csk to impose its inhibitory potential on these kinases. A role of PAG was initially seen in negative regulation of immune reactions. Since the year 2000 other Csk-dependent and independent interactions have been discovered and some of them showed anti-oncogenic effects in experiment. According to current opinions, these findings place PAG in a position of tumour suppressor candidate.
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Department of Cellular Pathology, James Cook University Hospital, Middlesbrough, United Kingdom. alexandr.svec@stees.nhs.uk
D048868:Adaptor Proteins, Signal Transducing / Q000502:physiology*; D000818:Animals; D002471:Cell Transformation, Neoplastic; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D015398:Signal Transduction; D025521:Tumor Suppressor Proteins / Q000502:physiology*; D019061:src-Family Kinases / Q000502:physiology
D048868:Adaptor Proteins, Signal Transducing; D008565:Membrane Proteins; C498710:PAG1 protein, human; D025521:Tumor Suppressor Proteins; D019061:src-Family Kinases