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TitleStructural mechanism for the recognition of E2F1 by the ubiquitin ligase adaptor Cyclin F.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 26, Page e2501057122, Year 2025
Publish dateJun 23, 2025
AuthorsPeter Ngoi / Xianxi Wang / Sivasankar Putta / Ricardo F Da Luz / Vitor Hugo B Serrão / Michael J Emanuele / Seth M Rubin /
PubMed AbstractCyclin F, a noncanonical member of the cyclin protein family, plays a critical role in regulating transitions in the cell division cycle. Unlike canonical cyclins, which bind and activate cyclin- ...Cyclin F, a noncanonical member of the cyclin protein family, plays a critical role in regulating transitions in the cell division cycle. Unlike canonical cyclins, which bind and activate cyclin-dependent kinases (CDKs), Cyclin F functions as a substrate receptor protein within the Skp1-Cullin-F-box E3 ubiquitin ligase complex, enabling the ubiquitylation of target proteins. The structural features that distinguish Cyclin F as a ligase adaptor and the mechanisms underlying its selective substrate recruitment over Cyclin A, which functions in complex with CDK2 at a similar time in the cell cycle, remain largely unexplored. We utilized single-particle cryoelectron microscopy to elucidate the structure of a Cyclin F-Skp1 complex bound to an E2F1 peptide. The structure and biochemical analysis reveal important differences in the substrate-binding site of Cyclin F compared to Cyclin A. Our findings expand on the canonical cyclin-binding motif (Cy or RxL) and highlight the importance of electrostatics at the E2F1 binding interface, which varies between Cyclin F and Cyclin A. These results advance our understanding of E2F1 regulation and may inform strategies for selectively targeting Cyclin F in cancer or neurodegeneration.
External linksProc Natl Acad Sci U S A / PubMed:40549918 / PubMed Central
MethodsEM (single particle)
Resolution3.47 Å
Structure data

45413

9cb3

EMDB-45413, PDB-9cb3:
E2F1-Cyclin F Interface
Method: EM (single particle) / Resolution: 3.47 Å

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / SCF Ubiquitin Ligase

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