A key activator of Ras signaling adopts an autoinhibited, dimeric conformation that is activated by membrane and calcium binding.

Genetically induced conformational modulation of eIF2B activates the Integrated Stress Response by impairing nucleotide exchange.

The Ras activator RasGRP1 that impacts Ras signals in immune cells, leukemias, and colorectal cancer, switches to an active conformation aided by a pH-sensitive histidine residue in a central location of the RasGRP1 molecule.

Building on previous work (Wang et al., 2014), it is shown that the nucleotide exchange factor of the chaperone BiP (Sil1) unexpectedly facilitates the reduction of oxidized BiP.

Genetic and proteomic screening with Wolbachia's CidB enzyme reveal the mechanisms and targets of cytoplasmic incompatibility (CI).

PDZ-RhoGEF controls adipose tissue abundance and whole body metabolism.

Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.

A drug-like molecule called ISRIB, which activates the translation initiation factor eIF2B, antagonizes stress responses as diverse as protein misfolding and nutrient deprivation, and restores protein synthesis, enhancing memory.

Understanding the complex auto-regulatory mechanisms for guanine nucleotide exchange factors is critically important for fully appreciating the layers of control for small GTPases.

The ciliary G-protein Arl13B – which is often mutated in Joubert syndrome – is the Guanine nucleotide exchange factor for the G-protein Arl3 and exclusively localizes to cilia.