Selective macroautophagy uses double-membrane vesicles, termed autophagosomes, 
to transport cytoplasmic pathogens, organelles and protein complexes to the 
vacuole for degradation. Autophagosomes are formed de novo by membrane fusion 
events at the phagophore assembly site (PAS). Therefore, precursor membrane 
material must be targeted and transported to the PAS. While some 
autophagy-related (Atg) proteins, such as Atg9 and Atg11, are known to be 
involved in this process, most of the mechanistic details are not understood. 
Previous work has also implicated the small Rab-family GTPase Ypt1 in the 
process, identifying Trs85 as a unique subunit of the TRAPPIII targeting complex 
and showing that it plays a macroautophagy-specific role; however, the 
relationship between Ypt1, Atg9 and Atg11 was not clear. Now, a recent report 
shows that Atg11 is a Trs85-specific effector of the Rab Ypt1, and may act as a 
classic coiled-coil membrane tether that targets Atg9-containing membranes to 
the PAS. Here, we review this finding in the context of what is known about 
Atg11, other Rab-dependent coiled-coil tethers, and other tethering complexes 
involved in autophagosome formation.