Cardiolipin, conformation, and respiratory complex-dependent oligomerization of the major mitochondrial ADP/ATP carrier in yeast

N. Senoo, S. Kandasamy, O. B. Ogunbona, M. G. Baile, Y. Lu, S. M. Claypool

Producción científica: Articlerevisión exhaustiva

30 Citas (Scopus)

Resumen

The phospholipid cardiolipin has pleiotropic structural and functional roles that are collectively essential for mitochondrial biology. Yet, the molecular details of how this lipid supports the structure and function of proteins and protein complexes are poorly understood. To address this property of cardiolipin, we use the mitochondrial adenosine 5'-diphosphate/adenosine 5'-triphosphate carrier (Aac) as a model. Here, we have determined that cardiolipin is critical for both the tertiary and quaternary assembly of the major yeast Aac isoform Aac2 as well as its conformation. Notably, these cardiolipin-provided structural roles are separable. In addition, we show that multiple copies of Aac2 engage in shared complexes that are largely dependent on the presence of assembled respiratory complexes III and IV or respiratory supercomplexes. Intriguingly, the assembly state of Aac2 is sensitive to its transport-related conformation. Together, these results expand our understanding of the numerous structural roles provided by cardiolipin for mitochondrial membrane proteins.

Idioma originalEnglish (US)
Número de artículoeabb0780
PublicaciónScience Advances
Volumen6
N.º35
DOI
EstadoPublished - ago 2020
Publicado de forma externa

ASJC Scopus subject areas

  • General

Huella

Profundice en los temas de investigación de 'Cardiolipin, conformation, and respiratory complex-dependent oligomerization of the major mitochondrial ADP/ATP carrier in yeast'. En conjunto forman una huella única.

Citar esto