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Coat complexes are diverse proteins that associate with forming or formed vesicles in secretory and endocytic membrane trafficking pathways. Coat complexes might provide structural stability, assist in cargo selection or vesicle budding, and influence directional transport.
How RNA polymerase II subunits enter the nucleus is not well understood. Here, the authors show that Transport and Golgi organization protein 6, TANGO6, recruits RNA polymerase II subunit B2, RPB2, to the ER membrane in a retrograde manner and transports it to the nucleus with the aid of importins.
The epidermal growth factor receptor (EGFR) plays important roles in cell growth and motility. Here, authors reveal an unexpected function for a metabolic enzyme PGK1 and advance the mechanistic understanding of lysosomal transport of EGFR.
Release of glutamate at high frequency involves a distinct subset of synaptic vesicles made by adaptor protein AP-3. Sorting of the phospholipid flippase ATP8A1 by AP-3 confers release at high frequency by recruiting synapsin to synaptic vesicles.
Cytosolic coat proteins capture secretory cargo and sculpt membrane carriers for intracellular transport, such as COPII which mediates Endoplasmic Reticulum to Golgi trafficking of thousands of cargoes. Here authors visualise the complete, membrane-assembled COPII coat by cryo-electron tomography and subtomogram averaging, revealing the full network of interactions within and between coat layers.
Hsu et al. find that the protein kinase Akt acts as a co-adaptor in the clathrin coat complex and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling.
Cargo-carrying vesicles can assemble from hundreds of locations on the cell membrane, but how these sites are selected has been unclear. A small family of membrane-sculpting proteins may select the perfect location.
