Quantitative 3D lattice light sheet microscopy of unperturbed cells combined with electron tomography and acute loss of function experiments reveals how dynamic ESCRT-III/Vps4 assemblies succeed in reverse membrane budding on endosomes.
Key sequence motifs, defined using the first reported structure of a monotopic membrane protein with a reentrant helix, enable identification of new monotopic membrane protein families previously predicted as membrane spanning.
Synthetic single domain antibody libraries and a binder selection cascade encompassing ribosome and phage display enable the selection of conformation-specific binders against previously intractable membrane proteins within three weeks.
Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.
Bioinformatics and experimental approaches identify families of membrane proteins requiring the co-ordinated action of the Sec pathway and Tat pathways for their integration and define features of the polypeptides that mediate interaction with these pathways.
Coarse-grained modeling reveals a new mechanism for multispanning membrane protein topogenesis, in which misintegrated configurations of the proteins undergo post-translational annealing to reach final, fully integrated multispanning topologies.
LAMP proteins, the major glycoproteins of the lysosome membrane, bind cholesterol directly and specifically, and interact with NPC1 and NPC2 proteins as part of the lysosomal cholesterol export process.