Activin class member, activin C, is a canonical TGFβ family member that signals through the type I receptor, action receptor-like kinase 7 and is resistant to follistatin antagonism.

RNA sequencing and conditional Nova mutants reveal that Nova protein function is necessary for activity-dependent alternative splicing of synaptic genes within somatostatin cortical interneurons and regulates its afferent and efferent connectivity.

CaMKII and the actin-crosslinking protein α-actinin-2 associate within minutes of the induction of long-term potentiation and disrupting this interaction prevents formation of enlarged dendritic spines.

Activation of Activin A-expressing progenitor cells emerges as a pivotal mechanism in bone fracture healing, shedding light on a potential therapeutic avenue to augment bone repair processes.

NODAL/Activin-induced SMAD2 binding directly drives remodeling of both open and closed chromatin and does not directly correlate with temporal patterns of gene expression upon prolonged signaling.

Computational simulations of actin network growth at the cell leading edge, combined with careful high-speed video microscopy measurements of leading edge shape fluctuations, suggest that Arp2/3 branching of the actin network occurs at an optimal angle to minimize fluctuations.

A mathematical model describes the function of dopaminergic neurons in both learning and action planning.

Sparse firing in a hippocampus-like structure of the teleost telencephalon is linked to spatial navigation and active sensing.

Cryo-EM structures of actomyosin VI in multiple nucleotide states reveal a unique actin-myosin interface and a mechanism of force-sensitivity; furthermore, myosin VI remodels F-actin, suggesting a role for actin structural plasticity during force generation.

Biophysical and structural studies reveal how low piconewton forces across actin enhance binding by the critical cell-cell adhesion protein α-catenin versus its force insensitive homolog vinculin.