Cellular waste, such as damaged organelles or protein aggregates, is targeted to the lysosome for degradation through the process of autophagy. Autophagy is known to occur through bulk sequestering of targets, observed during starvation, or through specific recognition of targets in selective autophagy. The family of TRIM proteins has emerging roles as receptor and platform proteins for autophagy regulators. In this paper (p. 3562), Michael A. Mandell, Vojo Deretic and co-workers demonstrate an unexpected dual function of TRIM17 in autophagy. The authors show that TRIM17 acts on targets – such as the p62 receptor – in a broad, selective and inhibitory manner. Furthermore, they report that it also selectively contributes to targeting the midbody – the multiprotein cytokinetic remnant found prior to abscission – for autophagic degradation. The inhibitory role of TRIM17 is linked to the assembly of the anti-autophagy factor Mcl-1 into a complex with the core autophagy regulator Beclin 1. When TRIM17 and Beclin1 are localized to the midbody, Mcl-1 dissociates from the complex. In the absence of its negative regulator Mcl-1, Beclin-1 then promotes midbody clearance with the help of additional TRIM proteins. This work provides an understanding of the selective removal of cellular components through autophagy, and a new autophagy mechanism of selective avoidance and targeted focusing through proteins of the TRIM family.

• © 2016. Published by The Company of Biologists Ltd