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Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

Alk5/TGF-β signaling is required in the endothelium to orchestrate zebrafish cardiac outflow tract morphogenesis, regulating smooth muscle cell and extracellular matrix organization.

Structure-function characterization of the EMC's cytoplasmic, transmembrane, and lumenal domains reveal features critical for terminal helix insertion and a specialized role for the lumenal domain in polytopic membrane protein biogenesis.

A membrane protein complex in the endoplasmic reticulum is a key factor for the biogenesis of multi-pass transmembrane proteins, including Rh1, and its loss causes retinal degeneration.

How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

To maintain genomic integrity during oocyte development, the tumor suppressor BRCA1/BRC-1 and the SMC-5/6 complex both repress intersister crossover recombination events while BRCA1/BRC-1 also specifically inhibits error prone repair of DNA breaks during meiotic prophase I.

By focusing on RNA-binding proteins whose genes have super enhancers in smooth muscle cells, the protein RBPMS was identified as an alternative splicing master regulator.

Chromosome condensation by condensin II is inhibited during interphase by direct interaction with MCPH1, which regulates opening of the condensin II interface between SMC2 and NCAPH2, in a similar fashion to how WAPL regulates Cohesin.

SMOC inhibits BMP signaling locally, but also expands the range of BMP signaling by competing for heparan sulfate binding sites.

Habituation to brief olfactory stimulation is biphasic and mediated by distinct neuronal circuits where an initial latency phase is rapidly followed by stimulus devaluation signifying behavioral habituation in Drosophila.