Ig Superfamily Ligand and Receptor Pairs Expressed in Synaptic Partners in Drosophila
Abstract
Information processing relies on precise patterns of synapses between neurons. The cellular recognition mechanisms regulating this specificity are poorly understood. In the medulla of the Drosophila visual system, different neurons form synaptic connections in different layers. Here, we sought to identify candidate cell recognition molecules underlying this specificity. Using RNA sequencing (RNA-seq), we show that neurons with different synaptic specificities express unique combinations of mRNAs encoding hundreds of cell surface and secreted proteins. Using RNA-seq and protein tagging, we demonstrate that 21 paralogs of the Dpr family, a subclass of immunoglobulin (Ig)-domain containing proteins, are expressed in unique combinations in homologous neurons with different layer-specific synaptic connections. Dpr interacting proteins (DIPs), comprising nine paralogs of another subclass of Ig-containing proteins, are expressed in a complementary layer-specific fashion in a subset of synaptic partners. We propose that pairs of Dpr/DIP paralogs contribute to layer-specific patterns of synaptic connectivity.
Additional Information
© 2015 Elsevier Inc. Received: April 23, 2015; Received in revised form: September 27, 2015; Accepted: November 10, 2015. Published: December 17, 2015. We thank Orkun Akin, John Carlson, Claude Desplan, Yasushi Hiromi, Frank Laski, Cheng-yu Lee for sharing reagents; members of our laboratory for discussion; Louis K. Scheffer and Ian Meinertzhagen for discussions, sharing results from the EM studies at Janelia Research Campus (HHMI) and comments on the manuscript; Kaushiki Menon and Robert Carrillo (Zinn group) for communicating results prior to publication; Donghui Cheng, Tanya Stoyanova and Owen Witte for assistance in FACS purification of cells; Dorian Gunning for generating Bsh antibody; and Barret Pfeiffer and Gerald Rubin (JRC/HHMI) for reagents to construct the markers for R7 neurons. The work was supported by a Graduate Student Fellowship from the China Scholarship Council (CSC) and a Graduate Student Fellowship from the University of California, Los Angeles (UCLA) Philip Whitcome Training Program (L.T.); the Canadian Institute of Health Research Fellowship (K.X.Z.); Jane Coffin Childs Memorial Fund for Medical Research (M.P.); the Robert A. and Renee E. Belfer Family Foundation (S.N.-J.); Target A.L.S. (P.-T.L.); a Long-Term Fellowship from the Human Frontiers Science Program (W.T.); grants from National Institute of Health (R01GM067858 (H.J.B.), R01NS62821 (K.Z.), and R01NS28182 (K.Z.); a Ramon y Cajal contract (RYC-2011-09479) and a Ministerio de Economia y Competitividad grant (BFU2012-32282) (M.M.). H.J.B. and S.L.Z. are investigators of Howard Hughes Medical Institute.Attached Files
Accepted Version - nihms768134.pdf
Supplemental Material - mmc1.pdf
Supplemental Material - mmc2.xls
Supplemental Material - mmc3.xlsx
Supplemental Material - mmc4.xlsx
Supplemental Material - mmc5.xlsx
Supplemental Material - mmc6.xlsx
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Additional details
- PMCID
- PMC4804707
- Eprint ID
- 63073
- DOI
- 10.1016/j.cell.2015.11.021
- Resolver ID
- CaltechAUTHORS:20151218-113427419
- China Scholarship Council
- University of California Los Angeles (UCLA)
- Canadian Institutes of Health Research (CIHR)
- Jane Coffin Childs Memorial Fund for Medical Research
- Robert A. and Renee E. Belfer Family Foundation
- Target ALS
- Human Frontiers Science Program
- NIH
- R01GM067858
- NIH
- R01NS62821
- NIH
- R01NS28182
- Ramon y Cajal
- RYC-2011-09479
- Ministerio de EconomÃa y Competitividad (MINECO)
- BFU2012-32282
- Howard Hughes Medical Institute (HHMI)
- Created
-
2015-12-19Created from EPrint's datestamp field
- Updated
-
2022-05-13Created from EPrint's last_modified field