Volume 28 Issue 3, March 2021

The highly conserved striatin-interacting phosphatase and kinase (STRIPAK) multimeric complex regulates the Hippo signaling pathway through phosphatase activity. A recent structure of the core STRIPAK hub reveals how striatins tetramerize to serve as a scaffolding platform for the assembly of an intricate architecture, which is distinct from that of all other protein phosphatase 2A (PP2A) complexes.

Recent structures of eukaryotic membrane protein insertases of the Oxa1 superfamily reveal a conserved protein module and common mechanistic principles that enable membrane insertion of a diverse set of substrates.

Cryo-EM structures of the enzyme complexes catalyzing the rate-limiting step in sphingolipid synthesis reveal mechanisms of substrate recognition and modulation by regulatory subunits.

Cryo-EM structures of serine palmitoyltransferase complexes mediating a key reaction of sphingolipid biosynthesis elucidate principles of its multimeric assembly, regulation and substrate selectivity

Structures of GPCR neurotensin receptor 1 (NTSR1) in complex with neurotensin and Gα_i1β₁γ₁ in a lipid bilayer environment and without stabilizing antibodies reveal extensive interactions at the GPCR–G protein interface.

Structural and functional analyses of BRCA1/BARD1 E3 ligase interactions with the H2A C-terminal tail reveal both the basis of its substrate specificity and the consequences of cancer-associated BRCA1/BARD1 mutations.

The mechanism behind Trim-Away, a protein-depletion approach using E3 ligase, TRIM21 and an antibody against the target, is now clarified, allowing expansion of the toolbox.

A cryo-EM structure of the striatin-interacting phosphatase and kinase (STRIPAK) complex reveals the overall architecture of this large, multisubunit assembly that broadly regulates different signaling pathways.

Cryo-EM structures of the Fanconi anemia core complex reveal insights into the remodeling of the FANCI–FANCD2 DNA clamp, which is essential during the repair of DNA interstrand crosslinks.

A new cryo-EM structure of the ~1 MDa Escherichia coli cellulose synthase macrocomplex reveals how cellulose biosynthesis and phosphoethanolamine (pEtN) modification are coupled to promote host-tissue adhesion.

The antiparasitic drug suramin directly inhibits SARS-CoV-2 RNA-dependent RNA polymerase by blocking binding of the RNA template–primer duplex and entry of nucleotide triphosphate to the catalytic site.