The interaction of SecA with its substrate proteins is regulated by its evolutionarily conserved C-terminal tail, which autoinhibits SecA unless SecA binds to the ribosome.

Hydrogen-deuterium exchange mass spectrometry reveals nucleotide-driven conformational regulation of Sec protein-channel to help impose directionality for protein transport through the Sec complex.

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

Mycobacterium tuberculosis (Mtb), effectors secreted through SecA2 pathway cause double strand breaks (DSBs) in the host DNA, which in turn activates ATM kinase to gain survival advantages, through Akt.

SatS of Mycobacterium tuberculosis is a new protein export chaperone with a role in exporting proteins by the specialized SecA2 pathway and a role in intracellular growth in macrophages.

Surface protein precursors traffic to lipoteichoic acid-rich septal membranes of Staphylococcus aureus for cleavage of their YSIRK-GXXS motif signal peptides and SecA-mediated translocation across the plasma membrane.

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

A damaging form of positive feedback linking elevated calcium levels and metabotropic glutamate receptor function in Purkinje neurons plays a critical role in the pathology in spinocerebellar ataxias.

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.

TBX5-loss associated cardiomyocyte ectopy and atrial fibrillation is prevented by augmentation of SERCA2 activity, establishing a mechanism underlying the genetic basis for a Ca²⁺-dependent pathway for AF risk.