Chlamydia hijacks membrane trafficking proteins of the human host via the cytoplasmic domain of a secreted transmembrane protein.

An unbiased proteomic approach identifies a new regulator of AMPA receptor trafficking providing additional insight into synaptic transmission and plasticity.

Structure of a pathogen effector complexed to Sorting Nexin 5 reveals an evolutionarily conserved interface that is required for retromer-dependent host restriction.

The yeast VARP homolog forms a new sorting nexin complex that promotes its own membrane recruitment through GEF activity and regulates the distribution of endosomal proteins.

The adaptive SNX32 regulates cargo sorting in neuronal and non-neuronal cells.

Sorting nexin 9, a membrane curvature inducing protein, creates a distinct environment within clusters of the co-receptor CD28 and thereby allows T cell activation to proceed to a successful outcome.

PX-BAR Mvp1 and dynamin-like GTPase Vps1 drive retromer-independent endosomal recycling.

The CDC25 family protein phosphatase Mih1 promotes downregulation of cell surface proteins in budding yeast by dephosphorylating a subunit of the retromer complex, which mediates plasma membrane recycling.

SNX4 influences synaptic vesicle recruitment at the active zone, linking endosomal sorting to docked vesicle density and modulating neurotransmission efficiency during sustained activity.

A novel role of endosomal machineries retromer and ESCRT in membrane delivery of Drosophila septate junction components is required for maintenance of junction integrity and epithelial barrier function.