RIT1 oncoproteins escape LZTR1-mediated proteolysis

See allHide authors and affiliations

Science  15 Mar 2019:
Vol. 363, Issue 6432, pp. 1226-1230
DOI: 10.1126/science.aav1444

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Defective degradation as disease mechanism

Ubiquitination often targets proteins for destruction. Castel et al. describe a mechanism by which mutations in the small guanine triphosphatase RIT1 may act to cause certain developmental disorders and cancers. They detected a protein, LZTR1, that interacted with wild-type RIT1 but not with oncogenic mutant forms of RIT1. LZTR1 acts as a substrate-specific adaptor for a ubiquitin ligase. Altered forms of RIT1 that are not subject to ubiquitin-mediated degradation thus accumulate. Because RIT1 functions in growth factor signaling and excessive signaling, these findings may explain the malignancies associated with RIT1 mutations.

Science, this issue p. 1226