Heterochromatin formation at transposon loci depends on dimerisation of the effector complex that elicits co-transcriptional silencing and this requirement is fulfilled by co-option of the conserved dimerisation hub protein, Cut-up/LC8.
An ensemble of the ubiquitin-activating enzyme UBA6 and ubiquitin-conjugating enzyme/ubiquitin-ligase BIRC6 mediates ubiquitination of LC3, targeting the latter for proteasomal degradation and thus attenuating autophagic degradation of cellular substrates.
Building on previous work (Ge et al., 2013), it is shown that the ER-Golgi intermediate compartment is a platform for the production of COPII vesicles as precursor membranes for the lipidation of LC3, which is an essential step in autophagosome biogenesis.
Binding of multiple LC8 copies to the intrinsically disordered region of the transcription factor ASCIZ exemplifies a new and potentially widespread molecular mechanism for negative feedback regulation.
A high-throughput comparison of substrate specificities of the Src-family kinases Lck and c-Src against a library of proteome-derived phosphorylation sites reveals that Lck has evolved divergent electrostatic features reflecting its involvement in T-cell signaling.
Innate lymphoid cells, which are dynamic under steady-state conditions, respond to a colitogenic stimulus by mobilizing from cryptopatches and secreting GM-CSF to organize the pro-inflammatory response.
The crystal structure of human WIPI2 bound to the ATG16L1 WIPI2-interacting region, combined with in vitro reconstitution and cellular autophagy assays, shows how the LC3 lipidation machinery is recruited in autophagy initiation.