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Point centromeres of budding yeast direct binding of a CBF3 complex that recruits the centromere-specific Cse4 nucleosome to CEN loci. A cryo-EM structure of CBF3 bound to its cognate CDEIII element and a model of the CBF3–Cse4–CEN complex reveal interactions underlying kinetochore assembly.

Here the authors describes a high-resolution cryo-EM structure of the anaphase-promoting complex (APC/C) revealing insights into regulation of its activity and identifying a zinc-binding site in the APC2 subunit.

The anaphase-promoting complex/cyclosome (APC/C) is a large E3 ligase that mediates ubiquitin-dependent proteolysis of cell cycle regulatory proteins; here the complete secondary structure architecture of human APC/C complexed with its coactivator CDH1 and substrate HSL1 is determined at 7.4 Å resolution, revealing allosteric changes induced by the coactivator that enhance affinity for UBCH10–ubiqutin.

A cryo-electron microscopy determination of the atomic structures of anaphase-promoting complex (APC/C)–coactivator complexes with either Emi1 or a UbcH10–ubiquitin conjugate.

Here, the authors determine the structure of the human outer kinetochore KMN network complex, showing that it forms an extended and rigid rod-like structure and that it exists in an auto-inhibited state which can be relieved by phosphorylation.

The eight-subunit augmin complex is required to nucleate branching microtubules and create a robust mitotic spindle during cell division. Here, the authors use cryo-EM, crosslinking mass spectrometry, and computational tools to build a structural model of the human augmin complex.

Cryo-electron microscopy structures of the Saccharomyces cerevisiae inner kinetochore complex provide insights into the interdependencies of constituent subcomplexes and the mechanism of centromeric nucleosome recognition.

The crystal structure of fission yeast mitotic checkpoint complex (MCC) reveals how MCC assembly is regulated and the molecular basis of anaphase-promoting complex (APC/C) inhibition by MCC.

Cryo-EM analyses provide a near-atomic view of the C. elegans securin–separase complex, with insights into the mechanism by which securin inhibits separase's protease activity.

The APC/C is a large multiprotein complex that functions as an E3 ubiquitin ligase to regulate the cell cycle. Here, the entire APC/C complex is reconstituted, and in combination with structural studies a pseudo-atomic model for 70% of the complex is provided. These results contribute towards a molecular understanding of the roles of individual subunits in APC/C assembly and their interactions with co-activators, substrates and regulatory proteins.

A high-resolution structure of a complex between the anaphase-promoting complex (APC/C) and the mitotic checkpoint complex (MCC) reveals how MCC interacts with and represses APC/C by obstructing substrate recognition and suppressing E3 ligase activity.

DOCK2 is a guanine nucleotide exchange factor (GEF) that activates RHO GTPases and interacts with ELMO1, which stimulates its GEF activity. Here, the authors provide mechanistic insights into how ELMO1 regulates DOCK2 activity by determining the structure of the DOCK2–ELMO1 binary complex representing the closed, auto-inhibited state and the DOCK2−ELMO1−RAC1 ternary complex structure, where DOCK2−ELMO1 adopts an open, active conformation.

Phosphorylation of the anaphase-promoting complex (APC/C) allows for its control by the co-activator Cdc20; a mechanism that has relevance to understanding the control of other large multimeric complexes by phosphorylation.

The anaphase promoting complex/cyclosome (APC/C) is a large multimeric ubiquitin E3 ligase that regulates the eukaryotic cell cycle in processes such as chromatid segregation and completion of mitosis. It catalyses the polyubiquitylation of a diverse array of mitotic regulatory proteins and targets them for proteasomal degradation. Target selection also involves a co-activator protein (either Cdc20 or Cdh1) together with core APC/C subunits. Here, a cryo-EM structure of APC/C^Chd1 bound to a D-box peptide substrate is presented. The structure provides important insight into the recognition and catalytic mechanism of APC/C substrates.

The crystal structure of an archaeal Rce1 protein has been determined; this protein represents a novel type of intramembrane protease, with a distinct architecture and catalytic site.