One aspect of my research program focuses on the biosynthesis of integral membrane proteins. One intriguing class of these proteins, the aptly named tail-anchors (TA), constitute an important and diverse group that are unable to be targeted via the co-translational SRP pathway. While this has been recognized for nearly twenty years, only recently have factors that target these proteins to the ER been identified. We have focused on structural and mechanistic studies of these proteins that, in yeast, form the GET pathway (Guided Entry of Tail-anchor proteins). The pathway, as we posit, begins with the binding of TA-proteins to a co-chaperone called Sgt2. From here, the substrate is handed off, in a regulated process, to the soluble ATPase Get3. Get3 then forms a stable complex with the TA and delivers the protein to the ER membrane. The interaction between Sgt2 and Get3 is bridged by a pair of proteins called Get4/Get5 that are critical to regulation of the process. We have characterized this complicated multi-step process using a number of biophysical tools. I will frame a discussion of the pathway from our unique structural perspective presenting insight revealed from new structures of complexes between these proteins. Furthermore, I will elaborate on the more complicated pathway in higher eukaryotes and the role that these proteins play triaging membrane proteins in the cytoplasm.