A structure of the ciliary inner junction at 3.6 Å resolution permits atomic modeling of six inner junction proteins and their interactions with acetylated lysine 40 loops of alpha tubulins.

Biochemical and genetic approaches revealed a posttranslational mechanism controlling the abundance of SUN2, a critical nuclear envelope protein.

The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.

A conserved mitochondrial inner membrane complex called MICOS works together with the mitochondrial lipid cardiolipin and respiratory complexes to direct the position, copy number and stabilization of cristae structures for efficient respiration.

Genome-wide RNA-seq analysis of single cells of the developing mouse endolymphatic sac reveals its molecular-cellular architecture and a model for salt and fluid absorption required for acquisition of normal inner ear structure and function.

Habitat loss rather than fragmentation per se can weaken the positive BEF relationship by reducing the percentage of grassland specialists in the community.

Interactions between Aim24 and the mitochondrial outer and inner membrane contact site complex (MICOS) are essential for mitochondrial ultrastructure, lipid composition and oxidative phosphorylation.

Ultrastructural and loss-of-function experiments show that oligodendrocyte-encoded Kir4.1 is located near active axonal structures, including within myelin inner tongue, and has critical functions to promote axonal activity and preserve integrity.

The pressure of fluid in the inner ear is controlled by opening of cellular valves in the endolymphatic sac to allow for regulated transepithelial fluid flow.

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.