MOSPD3 reads an FFNT motif to anchor ATG2A on the er

ATG2A and ATG2B are bridge-like lipid transfer proteins that carry glycerophospholipids from the endoplasmic reticulum (ER) to the expanding phagophore. The phagophore end of the bridge is well described, but how the ER end is held in place has remained unclear. Our recent study [1] identified MOSPD3, an atypical member of the VAMP-associated protein (VAP) family, as an ER receptor for ATG2A: its major sperm protein (MSP) domain captures an FFNT (two phenylalanines in a neutral tract) motif near the N terminus of ATG2A, whereas ATG2B is recruited redundantly by MOSPD1 and MOSPD3. These findings identify a receptor-based anchor at the ER end of the bridge and raise new questions about how it is organized and regulated.