RNA helicases of the DEAH/RHA family form a large and conserved class of enzymes 
that remodel RNA protein complexes (RNPs) by translocating along the RNA. Driven 
by ATP hydrolysis, they exert force to dissociate hybridized RNAs, dislocate 
bound proteins or unwind secondary structure elements in RNAs. The sub-cellular 
localization of DEAH-helicases and their concomitant association with different 
pathways in RNA metabolism, such as pre-mRNA splicing or ribosome biogenesis, 
can be guided by cofactor proteins that specifically recruit and simultaneously 
activate them. Here we review the mode of action of a large class of 
DEAH-specific adaptor proteins of the G-patch family. Defined only by their 
eponymous short glycine-rich motif, which is sufficient for helicase binding and 
stimulation, this family encompasses an immensely varied array of domain 
compositions and is linked to an equally diverse set of functions. G-patch 
proteins are conserved throughout eukaryotes and are even encoded within 
retroviruses. They are involved in mRNA, rRNA and snoRNA maturation, telomere 
maintenance and the innate immune response. Only recently was the structural and 
mechanistic basis for their helicase enhancing activity determined. We summarize 
the molecular and functional details of G-patch-mediated helicase regulation in 
their associated pathways and their involvement in human diseases.