The calcium channel subunit α2δ-3 organizes synapses via an activity-dependent and autocrine BMP signaling pathway

Kendall M. Hoover, Scott J. Gratz, Nova Qi, Kelsey A. Herrmann, Yizhou Liu, Jahci J. Perry-Richardson, Pamela J. Vanderzalm, Kate M. O’Connor-Giles and Heather T. Broihier ()
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Kendall M. Hoover: Case Western Reserve University School of Medicine
Scott J. Gratz: Brown University
Nova Qi: Case Western Reserve University School of Medicine
Kelsey A. Herrmann: Case Western Reserve University School of Medicine
Yizhou Liu: Case Western Reserve University School of Medicine
Jahci J. Perry-Richardson: Case Western Reserve University School of Medicine
Pamela J. Vanderzalm: University Heights
Kate M. O’Connor-Giles: Brown University
Heather T. Broihier: Case Western Reserve University School of Medicine

Nature Communications, 2019, vol. 10, issue 1, 1-18

Abstract: Abstract Synapses are highly specialized for neurotransmitter signaling, yet activity-dependent growth factor release also plays critical roles at synapses. While efficient neurotransmitter signaling relies on precise apposition of release sites and neurotransmitter receptors, molecular mechanisms enabling high-fidelity growth factor signaling within the synaptic microenvironment remain obscure. Here we show that the auxiliary calcium channel subunit α2δ-3 promotes the function of an activity-dependent autocrine Bone Morphogenetic Protein (BMP) signaling pathway at the Drosophila neuromuscular junction (NMJ). α2δ proteins have conserved synaptogenic activity, although how they execute this function has remained elusive. We find that α2δ-3 provides an extracellular scaffold for an autocrine BMP signal, suggesting a mechanistic framework for understanding α2δ’s conserved role in synapse organization. We further establish a transcriptional requirement for activity-dependent, autocrine BMP signaling in determining synapse density, structure, and function. We propose that activity-dependent, autocrine signals provide neurons with continuous feedback on their activity state for modulating both synapse structure and function.

Date: 2019
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DOI: 10.1038/s41467-019-13165-7

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