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Significance Many short-lived proteins perform important cellular functions that must be tightly regulated. EID1 is an unstable protein implicated in the control of transcription, differentiation, and genomic integrity. EID1 is particularly unstable in G0 cells. Here we show that an SCF complex containing the orphan F-box only protein FBXO21 is the ubiquitin ligase that recognizes EID1 in both cycling and G0 cells and that it recognizes a modular, peptidic domain within EID1. This degron overlaps with the EID1 region that binds to the retinoblastoma tumor suppressor protein (pRB) and to melanoma-associated antigen (MAGE) proteins, suggesting that multiple proteins compete for binding to EID1 and secondarily influence its ubiquitinylation. This study sheds light on the regulation of EID1, the function of FBXO21, and control of protein turnover by ubiquitin ligases.

Peptidic degron in EID1 is recognized by an SCF E3 ligase complex containing the orphan F-box protein FBXO21