Mitochondrial contact site and cristae organizing system promotes modular assembly of cytochrome c oxidase
Year: 2025
Type: article
Abstract: Mitochondrial cytochrome c oxidase, complex IV (CIV) of the respiratory chain, is assembled in a modular fashion from mitochondrial as well as nuclear-encoded subunits, guided by numerous assembly factors. This intricate process is further complicated by the characteristic architecture of the inner mitochondrial membrane. The mitochondrial contact site and cristae organizing system (MICOS) maintains the stability of crista junctions that connect the cristae, the site of mitochondrial respiration, with the inner boundary membrane, where newly imported respiratory subunits first arrive. Here, we report that MICOS facilitates specific assembly steps of CIV and associates with intermediates of the Cox1 and Cox3 modules. Moreover, MICOS recruits a variety of assembly factors even in the absence of ongoing CIV biogenesis, directly or via the mitochondrial multifunctional assembly (MIMAS). Our results establish MICOS as an important agent in efficient respiratory chain assembly that promotes CIV biogenesis within the compartmentalized inner membrane architecture.
Source: Cell Reports
Institutions: University of Freiburg, University of Bonn, Saarland University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,620
Awards: G1171311887, G2324002969, G3134524351, SFB 894: Ca2+Signale: Molekulare Mechanismen und Integrative Funktionen, FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala, G5225153069, Die Rolle der JDomänProteine in der Qualitätskontrolle des mitochondrialen Proteinimports, Die Rolle von Por1 und dessen Partnerprotein Om14 in mitochondrialem Proteinimport, SFB 1218: Regulation der zellulären Funktion durch Mitochondrien
OpenAlex ID: W4417485830