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TitleThe equilibrium between two quaternary assembly states determines the activity of SPOP and its cancer mutants.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJun 20, 2025
AuthorsMatthew J Cuneo / Ömer Güllülü / Mohamed-Raafet Ammar / Xinrui Gui / Kelly Churion / Martin Turk / Brian G O'Flynn / Nafiseh Sabri / Tanja Mittag /
PubMed AbstractProteostasis is critical for preventing oncogenesis. Both activating and inactivating mutations in the ubiquitin ligase subunit SPOP result in oncogenesis in different tissues. SPOP assembles into ...Proteostasis is critical for preventing oncogenesis. Both activating and inactivating mutations in the ubiquitin ligase subunit SPOP result in oncogenesis in different tissues. SPOP assembles into filaments that are multivalent for substrates, and substrates have multiple weak motifs for SPOP that are not activated via post-translational modifications. It is thus unclear how regulation is achieved. Here, we show that SPOP filaments circularize into rings that dimerize into up to 2.5 MDa-large, auto-inhibited double donuts. The equilibrium between double donuts and linear filaments determines SPOP activity. Activating and deactivating cancer mutations shift the equilibrium towards the filament or the double donut, respectively, and this influences substrate turnover and subcellular localization. This regulatory mechanism requires long filaments that can circularize into rings, likely explaining the presence of multiple weak SPOP-binding motifs in substrates. Activating and deactivating mutations combine to give rise to intermediate activities, suggesting new levers for cancer therapies.
External linksbioRxiv / PubMed:40666954 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 11.3 Å
Structure data

70881

9out

EMDB-70881, PDB-9out:
SPOP double donut locally refined MATH domains
Method: EM (single particle) / Resolution: 4.3 Å

70882

9ouu

EMDB-70882, PDB-9ouu:
SPOP double donut locally refined MATH domains
Method: EM (single particle) / Resolution: 4.3 Å

70883

9ouw

EMDB-70883, PDB-9ouw:
SPOP double donut locally refined MATH domains
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-71281: SPOP 12mer Double Donut
Method: EM (single particle) / Resolution: 10.7 Å

EMDB-71282: SPOP 13mer Double Donut
Method: EM (single particle) / Resolution: 9.44 Å

EMDB-71283: SPOP 14mer Double Donut
Method: EM (single particle) / Resolution: 11.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN BINDING / ubiquitination / protein degradation / protein oligomer / substrate adapter

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