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.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

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

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

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

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.

TNF-α treatment induces phosphorylation and cytoplasmic translocation of the retinoblastoma protein, which regulates cytoskeletal organization in skeletal muscle cells.

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.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.

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.