Abstract
A bacterial toxin that cleaves Ras oncoprotein.
Highlights
Rat sarcoma protein (Ras) mediates signal transduction from membrane receptors, such as epidermal growth factor receptor (EGFR), activating signaling cascades leading to phosphorylation of extracellular signal-regulated kinases (ERK1/2)
Mutated Ras has been found in 30% of human cancers, but with different distribution among Ras isoforms and cancer types
KRas-4B is mutated in 86% of human cancers, including pancreatic, lung, and colorectal carcinomas, while mutated NRas is almost exclusively found in melanomas [1]
Summary
Rat sarcoma protein (Ras) mediates signal transduction from membrane receptors, such as epidermal growth factor receptor (EGFR), activating signaling cascades leading to phosphorylation of extracellular signal-regulated kinases (ERK1/2). Several mutations have been demonstrated to impair Ras GTPase activity, residues G12V/C, G13V/D and Q61R are the most recurring Ras cancer mutations. This toxic effector domain was revealed in our recent paper published in Nature Communications to represent a new class of endopeptidase that processes Ras and Rap1 and was renamed RRSP for Ras/Rap1 specific peptidase [3].
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