Channel characteristics of the presequence translocation pore have a direct impact on protein import into the mitochondrial matrix.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

First two transmembrane segments of Tim17 are involved in interaction with the channel and the second two with the motor of the presequence translocase suggesting how proteins are handed over during their translocation into mitochondria.

A new approach measures the respective participations of elementary cell behaviors – such as cell division, intercalation, shape change and death – in the shaping of animal tissues.

The conserved polypeptide transport associated (POTRA) domains of the protein import channel, Toc75, are essential for protein import into chloroplasts.

The motor that drives preproteins into the mitochondrial matrix is coupled to the translocase by Tim44, a two-domain scaffold protein with an intrinsically disordered "dynamic arm" and a structurally stable anchoring domain.

Mechanical stimuli activate Piezo1 in osteoblast lineage cells and thereby promote bone formation in part via Wnt1.

A newly characterized calcium-activated chloride channel has been implicated in the immune system of Drosophila, shedding light on an enigmatic family of transmembrane proteins that are ubiquitous in nature.

Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.

Social isolation increases anti-social behaviour by altering activity in brain areas related to anxiety, stress, and reward.