How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

Evidence is presented that supports a completely new, diffusion-driven mechanism for transporting proteins across membranes in bacteria.

Asc1/RACK1 promotes the translation of mRNAs associated with the translational closed loop complex, which have short open reading frames and encode proteins required for core metabolic processes.

The heme and HRI-mediated eIF2aP–ATF4 integrated stress response in erythropoiesis has a major global impact, especially under the stress condition of iron deficiency.

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.

The retarding effect of a ribosome-bound internal ribosome entry site on eukaryotic protein synthesis is largely overcome following translocation of tripeptidyl-tRNA.

Ire1α co-opts the Sec61 translocon channel to efficiently cleave its mRNA substrates during endoplasmic reticulum stress conditions.

Development, validation, and use of an effector membrane translocation biosensor platform reveals G protein coupling selectivity signatures for 100 GPCRs that range from remarkable selectivity to full promiscuity toward the different G protein subtypes.

Mitochondria can tune the protein synthesis of nuclear-encoded proteins through condition-dependent mRNA localization that is regulated by translation elongation and the geometric constraints of the cell.

The complex process of protein translocation across membranes has been dissected into multiple key steps and the distributions of translocation rates indicate stochastic nature of the reaction.