Structure of MlaFB reveals how a small binding protein and the C-terminal tail on an ATPase subunit work together to regulate the assembly and function of an ABC transporter.
HIV-1 viral protein u (Vpu) can stimulate novel versions of canonical interactions with the clathrin adaptor AP1 to counteract the host antiviral protein BST2.
Cryo-EM reveals how a protein called NECAP inactivates the AP2 clathrin adaptor complex through concerted engagement of two domains which confer specificity for membrane-activated and phosphorylated AP2.
Polarity cascade initiated by aPKC in the periderm is transduced by adherens junction component E-cadherin to the basal epidermis during the development of zebrafish bilayered epidermis.
Single-turnover studies reveal quantitative insights into the inner mechanics and unfold hidden facets in the conformational coupling of ATP binding, hydrolysis, and substrate translocation by ABC transporters.
A heterodimeric exporter exhibits conformational equilibria in the presence of nucleotides, suggesting a unified mechanistic model for the conformational cycle of ABC exporters.
A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.