Journal
CELL
Volume 162, Issue 5, Pages 1140-1154Publisher
CELL PRESS
DOI: 10.1016/j.cell.2015.08.003
Keywords
-
Categories
Funding
- NIH [2RO1NS046747-05A1, 2P40OD010949-10A1]
- FWO [G059611N, G078913N, G077013N]
- BELSPO IUAP VII-20 WIBRAIN''
- VIB funding
- Boehringer Ingelheim Fonds
- EMBO
- JSPS
- SNSF
- NSF [IOS-1052555]
- National Center for Research Resources [P20RR016464, 5P20RR024210]
- NIGM from the NIH [8 P20 GM103554]
- DSHB
- HFSP
- Direct For Biological Sciences
- Division Of Integrative Organismal Systems [1052555] Funding Source: National Science Foundation
Ask authors/readers for more resources
Axonal branching contributes substantially to neuronal circuit complexity. Studies in Drosophila have shown that loss of Dscam1 receptor diversity can fully block axon branching in mechanosensory neurons. Here we report that cell-autonomous loss of the receptor tyrosine phosphatase 69D (RPTP69D) and loss of midline-localized Slit inhibit formation of specific axon collaterals through modulation of Dscam1 activity. Genetic and biochemical data support a model in which direct binding of Slit to Dscam1 enhances the interaction of Dscam1 with RPTP69D, stimulating Dscam1 dephosphorylation. Single-growth-cone imaging reveals that Slit/RPTP69D are not required for general branch initiation but instead promote the extension of specific axon collaterals. Hence, although regulation of intrinsic Dscam1-Dscam1 isoform interactions is essential for formation of all mechanosensory-axon branches, the local ligand-induced alterations of Dscam1 phosphorylation in distinct growth-cone compartments enable the spatial specificity of axon collateral formation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available