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Article

Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain.

The Biochemical journal - 1 Jul 2004

Rinaldi Teresa, Pick Elah, Gambadoro Alessia, Zilli Stefania, Maytal-Kivity Vered, Frontali Laura, Glickman Michael H

Abstract excerpt

Substrates destined for degradation by the 26 S proteasome are labelled with polyubiquitin chains. Rpn11/Mpr1, situated in the lid subcomplex, partakes in the processing of these chains or in their removal from substrates bound to the proteasome. Rpn11 also plays a role in maintaining mitochondrial integrity, tubular structure and proper function. The recent finding that Rpn11 participates in...

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Identifiers

PMID: 15018611
DOI: 10.1042/BJ20040008
PMCID: PMC1133786

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Participation of the proteasomal lid subunit Rpn11 in mitochondrial morphology and function is mapped to a distinct C-terminal domain.PMID 15018611Read ↗

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