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Regulation of axon repulsion by MAX-1 SUMOylation and AP-3
Journal article   Open access   Peer reviewed

Regulation of axon repulsion by MAX-1 SUMOylation and AP-3

Shih-Yu Chen, Chun-Ta Ho, Wei-Wen Liu, Mark Lucanic, Hsiu-Ming Shih, Pei-Hsin Huang and Hwai-Jong Cheng
Proceedings of the National Academy of Sciences - PNAS, v 115(35), pp E8236-E8245
28 Aug 2018
DOI: https://doi.org/10.1073/pnas.1804373115
PMID: 30104385
Featured in Collection :   UN Sustainable Development Goals @ Drexel
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https://doi.org/10.1073/pnas.1804373115View
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Abstract

Animals Axons - metabolism Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Protein Transport - physiology Sumoylation - physiology Transcription Factors - genetics Transcription Factors - metabolism
During neural development, growing axons express specific surface receptors in response to various environmental guidance cues. These axon guidance receptors are regulated through intracellular trafficking and degradation to enable navigating axons to reach their targets. In , the UNC-5 receptor is necessary for dorsal migration of developing motor axons. We previously found that MAX-1 is required for UNC-5-mediated axon repulsion, but its mechanism of action remained unclear. Here, we demonstrate that UNC-5-mediated axon repulsion in motor axons requires both SUMOylation and the AP-3 complex β subunit gene, Genetic interaction studies show that is SUMOylated by and acts upstream of Biochemical analysis suggests that constitutive interaction of MAX-1 and UNC-5 receptor is weakened by MAX-1 SUMOylation and by the presence of APB-3, a competitive interactor with UNC-5. Overexpression of APB-3 reroutes the trafficking of UNC-5 receptor into the lysosome for protein degradation. In vivo fluorescence recovery after photobleaching experiments shows that MAX-1 SUMOylation and APB-3 are required for proper trafficking of UNC-5 receptor in the axon. Our results demonstrate that SUMOylation of MAX-1 plays an important role in regulating AP-3-mediated trafficking and degradation of UNC-5 receptors during axon guidance.

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Web of Science research areas
Cell Biology
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