BMP-dependent synaptic development requires Abi-Abl-Rac signaling of BMP receptor macropinocytosis

Najin Kim, Sungdae Kim, Minyeop Nahm, Danielle Kopke, Joohyung Kim, Eunsang Cho, Min-Jung Lee, Mihye Lee, Seung Hyun Kim, Kendal Broadie and Seungbok Lee ()
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Najin Kim: Seoul National University
Sungdae Kim: Seoul National University
Minyeop Nahm: Hanyang University College of Medicine
Danielle Kopke: Vanderbilt Brain Institute, Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University
Joohyung Kim: Seoul National University
Eunsang Cho: Seoul National University
Min-Jung Lee: Seoul National University
Mihye Lee: Seoul National University
Seung Hyun Kim: Hanyang University College of Medicine
Kendal Broadie: Vanderbilt Brain Institute, Vanderbilt Kennedy Center for Research on Human Development, Vanderbilt University
Seungbok Lee: Seoul National University

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

Abstract: Abstract Retrograde BMP trans-synaptic signaling is essential for synaptic development. Despite the importance of endocytosis-regulated BMP receptor (BMPR) control of this developmental signaling, the mechanism remains unknown. Here, we provide evidence that Abelson interactor (Abi), a substrate for Abl kinase and component of the SCAR/WAVE complex, links Abl and Rac1 GTPase signaling to BMPR macropinocytosis to restrain BMP-mediated synaptic development. We find that Abi acts downstream of Abl and Rac1, and that BMP ligand Glass bottom boat (Gbb) induces macropinocytosis dependent on Rac1/SCAR signaling, Abl-mediated Abi phosphorylation, and BMPR activation. Macropinocytosis acts as the major internalization route for BMPRs at the synapse in a process driven by Gbb activation and resulting in receptor degradation. Key regulators of macropinocytosis (Rabankyrin and CtBP) control BMPR trafficking to limit BMP trans-synaptic signaling. We conclude that BMP-induced macropinocytosis acts as a BMPR homeostatic mechanism to regulate BMP-mediated synaptic development.

Date: 2019
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DOI: 10.1038/s41467-019-08533-2

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