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In addition, our in vitro studies indicate a novel mechanism, that is GSTP can be phosphorylated at Ser184 and enter the nucleus under LPS stimulation, and GSTP interacted with HMGB1 to inhibit cPKC-mediated phosphorylation of HMGB1 and association between HMGB1 and CRM1 in the nucleus
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Integrating of data from the Cancer Dependency Map revealed that 17% of the ERK phosphoproteome is critical for PDAC growth, confirming that ERK regulates the functions of cyclin-dependent kinases and the RAS homolog guanosine triphosphatase (RHO GTPase)
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