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TitleProbing the CRL4 interactions with MAGEA3 and CCT5 di-Glu C-terminal degrons.
Journal, issue, pagesPNAS Nexus, Vol. 3, Issue 4, Page pgae153, Year 2024
Publish dateApr 10, 2024
AuthorsGermanna Lima Righetto / Yanting Yin / David M Duda / Victoria Vu / Magdalena M Szewczyk / Hong Zeng / Yanjun Li / Peter Loppnau / Tony Mei / Yen-Yen Li / Alma Seitova / Aaron N Patrick / Jean-Francois Brazeau / Charu Chaudhry / Dalia Barsyte-Lovejoy / Vijayaratnam Santhakumar / Levon Halabelian /
PubMed AbstractDamaged DNA-binding protein-1 (DDB1)- and CUL4-associated factor 12 (DCAF12) serves as the substrate recognition component within the Cullin4-RING E3 ligase (CRL4) complex, capable of identifying C- ...Damaged DNA-binding protein-1 (DDB1)- and CUL4-associated factor 12 (DCAF12) serves as the substrate recognition component within the Cullin4-RING E3 ligase (CRL4) complex, capable of identifying C-terminal double-glutamic acid degrons to promote the degradation of specific substrates through the ubiquitin proteasome system. Melanoma-associated antigen 3 (MAGEA3) and T-complex protein 1 subunit epsilon (CCT5) proteins have been identified as cellular targets of DCAF12. To further characterize the interactions between DCAF12 and both MAGEA3 and CCT5, we developed a suite of biophysical and proximity-based cellular NanoBRET assays showing that the C-terminal degron peptides of both MAGEA3 and CCT5 form nanomolar affinity interactions with DCAF12 in vitro and in cells. Furthermore, we report here the 3.17 Å cryo-EM structure of DDB1-DCAF12-MAGEA3 complex revealing the key DCAF12 residues responsible for C-terminal degron recognition and binding. Our study provides new insights and tools to enable the discovery of small molecule handles targeting the WD40-repeat domain of DCAF12 for future proteolysis targeting chimera design and development.
External linksPNAS Nexus / PubMed:38665159 / PubMed Central
MethodsEM (single particle)
Resolution3.17 Å
Structure data

41105

8t9a

EMDB-41105, PDB-8t9a:
CryoEM structure of human DDB1-DCAF12 in complex with MAGEA3
Method: EM (single particle) / Resolution: 3.17 Å

Source
  • homo sapiens (human)
KeywordsLIGASE / DCAF12 / DNA damage-binding protein 1 / DDB1 / E3 ligase

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