Lamellar and tubular cristae in mitochondria form by two different molecular pathways that form both involve F1FO-ATP synthase dimers and the MICOS complex, but formation of lamellar cristae also relies on Mgm1/Opa1.
A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.
Building on previous work (Froelich et al., 2014), we present the X-ray crystal structure of an active MCM hexamer, which suggests a mechanism for MCM regulation and demonstrates a key interaction between the major domains.
An integrative approach, combining genetic mouse and large-scale human genetics studies, was used to reveal a novel role for the Bcl-2 protein Bid in maintenance of mitochondrial function that alters susceptibility to myocardial infarction.
A comprehensive analysis of the human MICOS complex has identified a novel subunit called QIL1 that is required for cristae junction formation in human cells and Drosophila, through its role in the assembly of the MICOS complex.
Crystal structures of γ-protocadherin cell-cell recognition dimers reveal the determinants of clustered protocadherin homophilic specificity and cis interaction region structures alongside mutagenesis data identify the putative cis interface.