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TitleStructural basis for the midnolin-proteasome pathway and its role in suppressing myeloma.
Journal, issue, pagesMol Cell, Vol. 85, Issue 13, Page 2597-2609.e11, Year 2025
Publish dateJul 3, 2025
AuthorsChristopher Nardone / Jingjing Gao / Hyuk-Soo Seo / Julian Mintseris / Lucy Ort / Matthew C J Yip / Milen Negasi / Anna K Besschetnova / Nolan Kamitaki / Steven P Gygi / Sirano Dhe-Paganon / Nikhil C Munshi / Mariateresa Fulciniti / Michael E Greenberg / Sichen Shao / Stephen J Elledge / Xin Gu /
PubMed AbstractThe midnolin-proteasome pathway degrades many nuclear proteins without ubiquitination, but how it operates mechanistically remains unclear. Here, we present structures of the midnolin-proteasome ...The midnolin-proteasome pathway degrades many nuclear proteins without ubiquitination, but how it operates mechanistically remains unclear. Here, we present structures of the midnolin-proteasome complex, revealing how established proteasomal components are repurposed to enable a unique form of proteolysis. While the proteasomal subunit PSMD2/Rpn1 binds to ubiquitinated or ubiquitin-like (Ubl) proteins, we discover that it also interacts with the midnolin nuclear localization sequence, elucidating how midnolin's activity is confined to the nucleus. Likewise, PSMD14/Rpn11, an enzyme that normally cleaves ubiquitin chains, surprisingly functions non-enzymatically as a receptor for the midnolin Ubl domain, positioning the substrate-binding Catch domain directly above the proteasomal entry site to guide substrates into the proteasome. Moreover, we demonstrate that midnolin downregulation is critical for the survival of myeloma cells by stabilizing the transcription factor substrate IRF4. Our findings uncover the mechanisms underlying the midnolin-proteasome pathway and midnolin downregulation as a driver of multiple myeloma.
External linksMol Cell / PubMed:40532701 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.9 Å
Structure data

44910

9bui

EMDB-44910, PDB-9bui:
M1A Midnolin-Proteasome (with Ubl)
Method: EM (single particle) / Resolution: 3.9 Å

44927

9bv1

EMDB-44927, PDB-9bv1:
M2A Midnolin-Proteasome (translocating)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-44928: M2A Midnolin Proteasome (translocating, focused on PSMD2)
Method: EM (single particle) / Resolution: 3.0 Å

44929

9bv2

EMDB-44929, PDB-9bv2:
M2B Midnolin-Proteasome (translocating)
Method: EM (single particle) / Resolution: 3.4 Å

44930

9bv3

EMDB-44930, PDB-9bv3:
M1B Midnolin-Proteasome
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsNUCLEAR PROTEIN / proteasome

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