In budding yeast, Get4 is part of the GET complex that inserts the tail-anchored (TA) proteins into the endoplasmic reticulum membrane [, ]. In humans, Get4 is part the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and facilitates their proper delivery to the endoplasmic reticulum, or alternatively promotes their sorting to the proteasome where they undergo degradation [, , , ]. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane [, , ].
This entry represents the binding domain at the N terminus of Mdy2 (also known as Get5) that binds to Get4. Together with Get3, this tripartite complex is involved in the insertion of tail-anchored proteins in the ER membrane [].
This entry represents a short N-terminal domain at the start of small glutamine-rich tetratricopeptide repeat-containing protein (SGTA), a heat-shock protein (HSP) co-chaperone involvedin the targeting of tail-anchor membrane proteins to the endoplasmic reticulum. This is the homodimerisation domain that mediates the association with a single copy of Get4 or Get5 proteins, providing a link to the rest of the GET pathway [].
Tail-anchored trans-membrane proteins are targeted to membranes post-translationally. The proteins Get4 and Get5 form an obligate complex that catalyzes the transfer of tail-anchored proteins destined to the endoplasmic reticulum from Sgt2 to the cytosolic targeting factor Get3. This is the carboxyl domain of Get5 (also known as Mdy2), a homodimerization domain, resulting in a heterotetrameric Get4/Get5 complex [].
