A comprehensive analysis of the human MICOS complex has identified a novel subunit called QIL1 that is required for cristae junction formation in human cells and Drosophila, through its role in the assembly of the MICOS complex.
Single-cell RNA sequencing of Drosophila hemocytes in blood distinguishes various states within known blood cell types and implicates a novel role for fibroblast growth factor receptor signaling in inter-hemocyte crosstalk.
Crystal structures of synaptic recognition molecules Sidekick-1 and -2 reveal a single homodimer interaction mode responsible for both cell-cell recognition and cis-clustering, suggesting that competition between cis and trans interactions may be critical to specificity.
Fly protein families Dprs and DIPs can create a multitude of complementary interfaces for homo- and heterophilic adhesion complexes, resulting in instructive roles for connectivity in the motor neuron circuitry.
The crystal structure of a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.
Crystal structures of γ-protocadherin cell-cell recognition dimers reveal the determinants of clustered protocadherin homophilic specificity and cis interaction region structures alongside mutagenesis data identify the putative cis interface.