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TitleNUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 9, Page 1752-1765, Year 2025
Publish dateApr 11, 2025
AuthorsConnor Arkinson / Ken C Dong / Christine L Gee / Shawn M Costello / Aimee Chi Soe / Greg L Hura / Susan Marqusee / Andreas Martin /
PubMed AbstractThe ubiquitin-like modifier FAT10 targets hundreds of proteins in the mammalian immune system to the 26S proteasome for degradation. This degradation pathway requires the cofactor NUB1, yet the ...The ubiquitin-like modifier FAT10 targets hundreds of proteins in the mammalian immune system to the 26S proteasome for degradation. This degradation pathway requires the cofactor NUB1, yet the underlying mechanisms remain unknown. Here, we reconstituted a minimal in vitro system with human components and revealed that NUB1 uses the intrinsic instability of FAT10 to trap its N-terminal ubiquitin-like domain in an unfolded state and deliver it to the 26S proteasome for engagement, allowing the degradation of FAT10-ylated substrates in a ubiquitin-independent and p97-independent manner. Using hydrogen-deuterium exchange, structural modeling and site-directed mutagenesis, we identified the formation of an intricate complex with FAT10 that activates NUB1 for docking to the 26S proteasome, and our cryo-EM studies visualized the highly dynamic NUB1 complex bound to the proteasomal Rpn1 subunit during FAT10 delivery and the early stages of ATP-dependent degradation. These findings identified a previously unknown mode of cofactor-mediated, ubiquitin-independent substrate delivery to the 26S proteasome that relies on trapping partially unfolded states for engagement by the proteasomal ATPase motor.
External linksNat Struct Mol Biol / PubMed:40217121 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.1 Å
Structure data

42506

8usb

EMDB-42506, PDB-8usb:
Non-substrate-engaged human 26S proteasome with Nub1/FAT10 bound to Rpn1
Method: EM (single particle) / Resolution: 2.73 Å

42507

8usc

EMDB-42507, PDB-8usc:
Nub1/Fat10-processing human 26S proteasome
Method: EM (single particle) / Resolution: 3.1 Å

42508

8usd

EMDB-42508, PDB-8usd:
Rpn1/Nub1UBL-focused alignment of the non-substrate-engaged human 26S proteasome
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE/PROTEIN BINDING / 26S protease complex / Nub1 / FAT10 / MOTOR PROTEIN / HYDROLASE-PROTEIN BINDING complex / 26S Proteasome

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