Autophagy requires several specific proteins, the Atg proteins, but also requires transport of membrane vesicles to the phagophore assembly site (PAS). In yeast, many small GTP-binding proteins, membrane traffic regulators, are essential for different stages of autophagy, from the formation of the autophagosome to the fusion of the autophagosome and the vacuole (Yang and Rosenwald 2014). We recently discovered that two small GTP-binding proteins, Arl1, a member of the Arf/Arl/Sar family, and Ypt6, a member of the Rab family, have novel roles in autophagy in S. cerevisiae (Yang and Rosenwald 2016). Both regulate membrane traffic between the trans-Golgi network (TGN) and endosomes. ARL1 and YPT6 also show synthetic lethality with one another, suggesting the encoded proteins have functional similarities (Costanzo et al. 2010). Mutants lacking one or the other of these genes have similar phenotypes; both the arl1Δ and ypt6Δ strains are unable to grow in the presence of rapamycin and perform autophagy, but only at high temperature (37°). We determined that the high temperature defect is caused by a failure to recruit the Golgi-associated retrograde protein (GARP) complex to the PAS in the absence of arl1Δ or ypt6Δ at 37°. The GARP complex is responsible for recruiting the SNARE Tlg2 to the PAS to deliver membranes derived from the Golgi apparatus to the growing phagophore (Reggiori et al. 2003).