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.

The conformational cycle of an ABC heterodimeric transporter reveals a divergence in the structural mechanism of ABC exporters.

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.

The most recent common ancestor of humans, chimpanzees, and bonobos possessed a foot adapted to terrestrial quadrupedalism and climbing.

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.

Endocytosis is regulated by a protein family that recycles the AP2 clathrin adaptor by restoring the inactive form of complex.