The non-signaling complex formed by Activin A and ACVR1 is operant in vivo and is required to temper the degree of heterotopic ossification in the genetic disorder fibrodysplasia ossificans progressiva.

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.

Combination of in vitro and in vivo approaches reveal how learning suppresses the microRNA system to trigger de novo synthesis of plasticity proteins, a missing link in the current model of microRNA-mediated translation in persistent synaptic plasticity and memory.

The activin receptor ALK7 regulates the adaptation of brown adipose tissue to nutrient availability by preventing over-activation of signaling pathways induced by fasting, allowing appropriate response to cold exposure.

The human Fibrodysplasia-Ossificans-Progressiva BMP-receptor mutant signals in zebrafish in the absence of ligand-binding, displays BMP ligand-responsive hyperactivity, neither requiring other type-I-BMP receptors, unlike wild-type, challenging views of the pathological mechanism.

A subset of the zebrafish Nodal receptor complex is regulated by positive feedback and controls the diffusion and distribution of Nodal signals during germ layer formation.

Live cell imaging demonstrates that the dynamics of ligand presentation influence signaling through two closely related morphogen signaling pathways in dramatically different ways.

Ligand capture by cell surface receptor complexes sets the shape of the Nodal signaling pattern in zebrafish.

Afferent-derived factors control the elaboration of appropriate and robust sizes of dendritic arbors by dynamically modulating dendritic growth parameters.

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.