Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 242

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Specification of synaptic connectivity by cell surface interactions

de Wit, Joris, Ghosh, Anirvan·2016·Nature Reviews Neuroscience

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nrn.2015.3

Cites

24 of 24 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 138

  1. Sanes, J. R. & Yamagata, M. Many paths to synaptic specificity. Annu. Rev. Cell Dev. Biol. 25, 161–195 (2009). · DOI
  2. Langley, J. N. Note on regeneration of prae-ganglionic fibres of the sympathetic. J. Physiol. 18, 280–284 (1895). · DOI
  3. Sperry, R. W. Chemoaffinity in the orderly growth of nerve fiber patterns and connections. Proc. Natl Acad. Sci. USA 50, 703–710 (1963). · DOI
  4. Yogev, S. & Shen, K. Cellular and molecular mechanisms of synaptic specificity. Annu. Rev. Cell Dev. Biol. 30, 417–437 (2014). · DOI
  5. Christensen, R., Shao, Z. & Colon-Ramos, D. A. The cell biology of synaptic specificity during development. Curr. Opin. Neurobiol. 23, 1018–1026 (2013). · DOI
  6. Williams, M. E., de Wit, J. & Ghosh, A. Molecular mechanisms of synaptic specificity in developing neural circuits. Neuron 68, 9–18 (2010). · DOI
  7. Sanes, J. R. & Zipursky, S. L. Design principles of insect and vertebrate visual systems. Neuron 66, 15–36 (2010). · DOI
  8. Colon-Ramos, D. A. Synapse formation in developing neural circuits. Curr. Top. Dev. Biol. 87, 53–79 (2009). · DOI
  9. Margeta, M. A., Shen, K. & Grill, B. Building a synapse: lessons on synaptic specificity and presynaptic assembly from the nematode C. elegans. Curr. Opin. Neurobiol. 18, 69–76 (2008). · DOI
  10. Takeichi, M. The cadherin superfamily in neuronal connections and interactions. Nat. Rev. Neurosci. 8, 11–20 (2007). · DOI
  11. Nollet, F., Kools, P. & van Roy, F. Phylogenetic analysis of the cadherin superfamily allows identification of six major subfamilies besides several solitary members. J. Mol. Biol. 299, 551–572 (2000). · DOI
  12. Hirano, S. & Takeichi, M. Cadherins in brain morphogenesis and wiring. Physiol. Rev. 92, 597–634 (2012). · DOI
  13. Weiner, J. A. & Jontes, J. D. Protocadherins, not prototypical: a complex tale of their interactions, expression, and functions. Front. Mol. Neurosci. 6, 4 (2013).
  14. Patel, S. D., Chen, C. P., Bahna, F., Honig, B. & Shapiro, L. Cadherin-mediated cell–cell adhesion: sticking together as a family. Curr. Opin. Struct. Biol. 13, 690–698 (2003). · DOI
  15. Patel, S. D. et al. Type II cadherin ectodomain structures: implications for classical cadherin specificity. Cell 124, 1255–1268 (2006). · DOI
  16. Nose, A., Tsuji, K. & Takeichi, M. Localization of specificity determining sites in cadherin cell adhesion molecules. Cell 61, 147–155 (1990). · DOI
  17. Klingelhofer, J., Troyanovsky, R. B., Laur, O. Y. & Troyanovsky, S. Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions. J. Cell Sci. 113, 2829–2836 (2000). · DOI
  18. Sano, K. et al. Protocadherins: a large family of cadherin-related molecules in central nervous system. EMBO J. 12, 2249–2256 (1993). · DOI
  19. Kim, S. Y., Yasuda, S., Tanaka, H., Yamagata, K. & Kim, H. Non-clustered protocadherin. Cell Adh. Migr. 5, 97–105 (2011). · DOI
  20. Chen, W. V. & Maniatis, T. Clustered protocadherins. Development 140, 3297–3302 (2013). · DOI
  21. Morishita, H. & Yagi, T. Protocadherin family: diversity, structure, and function. Curr. Opin. Cell Biol. 19, 584–592 (2007). · DOI
  22. Wu, Q. & Maniatis, T. A striking organization of a large family of human neural cadherin-like cell adhesion genes. Cell 97, 779–790 (1999). · DOI
  23. Maniatis, T. & Tasic, B. Alternative pre-mRNA splicing and proteome expansion in metazoans. Nature 418, 236–243 (2002). · DOI
  24. Wang, X., Su, H. & Bradley, A. Molecular mechanisms governing Pcdh-γ gene expression: evidence for a multiple promoter and cis-alternative splicing model. Genes Dev. 16, 1890–1905 (2002). · DOI
  25. Schreiner, D. & Weiner, J. A. Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion. Proc. Natl Acad. Sci. USA 107, 14893–14898 (2010). · DOI
  26. Thu, C. A. et al. Single-cell identity generated by combinatorial homophilic interactions between α, β, and γ protocadherins. Cell 158, 1045–1059 (2014). · DOI
  27. Han, M. H., Lin, C., Meng, S. & Wang, X. Proteomics analysis reveals overlapping functions of clustered protocadherins. Mol. Cell. Proteomics 9, 71–83 (2010). · DOI
  28. Li, Y. et al. Molecular and functional interaction between protocadherin γ-C5 and GABAA receptors. J. Neurosci. 32, 11780–11797 (2012). · DOI
  29. Ushkaryov, Y. A., Petrenko, A. G., Geppert, M. & Sudhof, T. C. Neurexins: synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science 257, 50–56 (1992). · DOI
  30. Ullrich, B., Ushkaryov, Y. A. & Sudhof, T. C. Cartography of neurexins: more than 1000 isoforms generated by alternative splicing and expressed in distinct subsets of neurons. Neuron 14, 497–507 (1995). · DOI
  31. Rowen, L. et al. Analysis of the human neurexin genes: alternative splicing and the generation of protein diversity. Genomics 79, 587–597 (2002). · DOI
  32. Schreiner, D. et al. Targeted combinatorial alternative splicing generates brain region-specific repertoires of neurexins. Neuron 84, 386–398 (2014). References 35 and 36 use deep-sequencing analyses of neurexin mRNAs to identify a novel splice site in neurexin, to generate a quantitative description of neurexin isoform diversity in the brain and to demonstrate that neurexin diversity is linked to cellular diversity. · DOI
  33. Ichtchenko, K. et al. Neuroligin 1: a splice site-specific ligand for β-neurexins. Cell 81, 435–443 (1995). · DOI
  34. Chih, B., Engelman, H. & Scheiffele, P. Control of excitatory and inhibitory synapse formation by neuroligins. Science 307, 1324–1328 (2005). · DOI
  35. Graf, E. R., Zhang, X., Jin, S. X., Linhoff, M. W. & Craig, A. M. Neurexins induce differentiation of GABA and glutamate postsynaptic specializations via neuroligins. Cell 119, 1013–1026 (2004). · DOI
  36. Krueger, D. D., Tuffy, L. P., Papadopoulos, T. & Brose, N. The role of neurexins and neuroligins in the formation, maturation, and function of vertebrate synapses. Curr. Opin. Neurobiol. 22, 412–422 (2012). · DOI
  37. Siddiqui, T. J. & Craig, A. M. Synaptic organizing complexes. Curr. Opin. Neurobiol. 21, 132–143 (2010). · DOI
  38. de Wit, J. et al. LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation. Neuron 64, 799–806 (2009). · DOI
  39. Ko, J., Fuccillo, M. V., Malenka, R. C. & Sudhof, T. C. LRRTM2 functions as a neurexin ligand in promoting excitatory synapse formation. Neuron 64, 791–798 (2009). · DOI
  40. Siddiqui, T. J., Pancaroglu, R., Kang, Y., Rooyakkers, A. & Craig, A. M. LRRTMs and neuroligins bind neurexins with a differential code to cooperate in glutamate synapse development. J. Neurosci. 30, 7495–7506 (2010). · DOI
  41. Pettem, K. L. et al. The specific α-neurexin interactor calsyntenin-3 promotes excitatory and inhibitory synapse development. Neuron 80, 113–128 (2013). · DOI
  42. Sugita, S. et al. A stoichiometric complex of neurexins and dystroglycan in brain. J. Cell Biol. 154, 435–445 (2001). · DOI
  43. Boucard, A. A., Ko, J. & Sudhof, T. C. High affinity neurexin binding to cell adhesion G-protein-coupled receptor CIRL1/latrophilin-1 produces an intercellular adhesion complex. J. Biol. Chem. 287, 9399–9413 (2012). · DOI
  44. Zhang, C. et al. Neurexins physically and functionally interact with GABAA receptors. Neuron 66, 403–416 (2010). · DOI
  45. Missler, M., Hammer, R. E. & Sudhof, T. C. Neurexophilin binding to α-neurexins. A single LNS domain functions as an independently folding ligand–binding unit. J. Biol. Chem. 273, 34716–34723 (1998). · DOI
  46. Petrenko, A. G. et al. Structure and evolution of neurexophilin. J. Neurosci. 16, 4360–4369 (1996). · DOI
  47. Uemura, T. et al. Trans-synaptic interaction of GluRδ2 and Neurexin through Cbln1 mediates synapse formation in the cerebellum. Cell 141, 1068–1079 (2010). · DOI · Paper page
  48. Boucard, A. A., Chubykin, A. A., Comoletti, D., Taylor, P. & Sudhof, T. C. A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to α- and β-neurexins. Neuron 48, 229–236 (2005). · DOI · Paper page
  49. Schreiner, D., Simicevic, J., Ahrne, E., Schmidt, A. & Scheiffele, P. Quantitative isoform-profiling of highly diversified recognition molecules. eLife 4, e07794 (2015). · DOI
  50. Dolan, J. et al. The extracellular leucine-rich repeat superfamily; a comparative survey and analysis of evolutionary relationships and expression patterns. BMC Genomics 8, 320 (2007). · DOI
  51. de Wit, J., Hong, W., Luo, L. & Ghosh, A. Role of leucine-rich repeat proteins in the development and function of neural circuits. Annu. Rev. Cell Dev. Biol. 27, 697–729 (2011). · DOI
  52. de Wit, J. & Ghosh, A. Control of neural circuit formation by leucine-rich repeat proteins. Trends Neurosci. 37, 539–550 (2014). · DOI
  53. de Wit, J. et al. Unbiased discovery of glypican as a receptor for LRRTM4 in regulating excitatory synapse development. Neuron 79, 696–711 (2013). · DOI
  54. Siddiqui, T. J. et al. An LRRTM4–HSPG complex mediates excitatory synapse development on dentate gyrus granule cells. Neuron 79, 680–695 (2013). · DOI
  55. O'Sullivan, M. L. et al. FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development. Neuron 73, 903–910 (2012). · DOI
  56. Kim, S. et al.NGL family PSD-95–interacting adhesion molecules regulate excitatory synapse formation. Nat. Neurosci. 9, 1294–1301 (2006). · DOI
  57. Barclay, A. N. Membrane proteins with immunoglobulin-like domains—a master superfamily of interaction molecules. Semin. Immunol. 15, 215–223 (2003). · DOI
  58. Yamagata, M. & Sanes, J. R. Expanding the Ig superfamily code for laminar specificity in retina: expression and role of contactins. J. Neurosci. 32, 14402–14414 (2012). · DOI
  59. Inoue, T., Tanaka, T., Suzuki, S. C. & Takeichi, M. Cadherin-6 in the developing mouse brain: expression along restricted connection systems and synaptic localization suggest a potential role in neuronal circuitry. Dev. Dyn. 211, 338–351 (1998). · DOI
  60. Suzuki, S. C., Inoue, T., Kimura, Y., Tanaka, T. & Takeichi, M. Neuronal circuits are subdivided by differential expression of type-II classic cadherins in postnatal mouse brains. Mol. Cell. Neurosci. 9, 433–447 (1997). · DOI
  61. Hertel, N., Redies, C. & Medina, L. Cadherin expression delineates the divisions of the postnatal and adult mouse amygdala. J. Comp. Neurol. 520, 3982–4012 (2012). · DOI
  62. Hertel, N., Krishna, K., Nuernberger, M. & Redies, C. A cadherin-based code for the divisions of the mouse basal ganglia. J. Comp. Neurol. 508, 511–528 (2008). · DOI
  63. Krishna, K. K., Hertel, N. & Redies, C. Cadherin expression in the somatosensory cortex: evidence for a combinatorial molecular code at the single-cell level. Neuroscience 175, 37–48 (2011). · DOI
  64. Krishna, K., Nuernberger, M., Weth, F. & Redies, C. Layer-specific expression of multiple cadherins in the developing visual cortex (V1) of the ferret. Cereb. Cortex 19, 388–401 (2009). · DOI
  65. Bekirov, I. H., Needleman, L. A., Zhang, W. & Benson, D. L. Identification and localization of multiple classic cadherins in developing rat limbic system. Neuroscience 115, 213–227 (2002). · DOI
  66. Huntley, G. W. et al. Synaptic loss and retention of different classic cadherins with LTP-associated synaptic structural remodeling in vivo. Hippocampus 22, 17–28 (2012). · DOI
  67. Bozdagi, O., Shan, W., Tanaka, H., Benson, D. L. & Huntley, G. W. Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation. Neuron 28, 245–259 (2000). · DOI
  68. Uchida, N., Honjo, Y., Johnson, K. R., Wheelock, M. J. & Takeichi, M. The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones. J. Cell Biol. 135, 767–779 (1996). · DOI · Paper page
  69. Benson, D. L. & Tanaka, H. N-cadherin redistribution during synaptogenesis in hippocampal neurons. J. Neurosci. 18, 6892–6904 (1998). · DOI
  70. Fannon, A. M. & Colman, D. R. A model for central synaptic junctional complex formation based on the differential adhesive specificities of the cadherins. Neuron 17, 423–434 (1996). · DOI
  71. Redies, C. & Takeichi, M. Cadherins in the developing central nervous system: an adhesive code for segmental and functional subdivisions. Dev. Biol. 180, 413–423 (1996). · DOI
  72. Basu, R., Taylor, M. R. & Williams, M. E. The classic cadherins in synaptic specificity. Cell Adh. Migr. 9, 193–201 (2015). · DOI
  73. Kohmura, N. et al. Diversity revealed by a novel family of cadherins expressed in neurons at a synaptic complex. Neuron 20, 1137–1151 (1998). · DOI
  74. Frank, M. et al. Differential expression of individual γ-protocadherins during mouse brain development. Mol. Cell. Neurosci. 29, 603–616 (2005). · DOI · Paper page
  75. Wang, X. et al. Gamma protocadherins are required for survival of spinal interneurons. Neuron 36, 843–854 (2002). · DOI
  76. Zou, C., Huang, W., Ying, G. & Wu, Q. Sequence analysis and expression mapping of the rat clustered protocadherin gene repertoires. Neuroscience 144, 579–603 (2007). · DOI
  77. Esumi, S. et al. Monoallelic yet combinatorial expression of variable exons of the protocadherin-α gene cluster in single neurons. Nat. Genet. 37, 171–176 (2005). · DOI
  78. Hirano, K. et al. Single-neuron diversity generated by Protocadherin-β cluster in mouse central and peripheral nervous systems. Front. Mol. Neurosci. 5, 90 (2012). · DOI
  79. Kaneko, R. et al. Allelic gene regulation of Pcdh-α and Pcdh-γ clusters involving both monoallelic and biallelic expression in single Purkinje cells. J. Biol. Chem. 281, 30551–30560 (2006). · DOI
  80. Hattori, D., Millard, S. S., Wojtowicz, W. M. & Zipursky, S. L. Dscam-mediated cell recognition regulates neural circuit formation. Annu. Rev. Cell Dev. Biol. 24, 597–620 (2008). · DOI
  81. Zipursky, S. L. & Sanes, J. R. Chemoaffinity revisited: Dscams, protocadherins, and neural circuit assembly. Cell 143, 343–353 (2010). · DOI
  82. Li, Y. et al. Synaptic and nonsynaptic localization of protocadherin γ-C5 in the rat brain. J. Comp. Neurol. 518, 3439–3463 (2010). · DOI
  83. Fuccillo, M. V. et al. Single-cell mRNA profiling reveals cell-type-specific expression of neurexin isoforms. Neuron 87, 326–340 (2015). This study profiles mRNAs isolated from single cells and finds cell type-specific expression of neurexin isoforms and neurexin ligands, supporting the existence of cell type-specific adhesion repertoires. · DOI
  84. Yamagata, M. & Sanes, J. R. Dscam and Sidekick proteins direct lamina-specific synaptic connections in vertebrate retina. Nature 451, 465–469 (2008). · DOI
  85. Yamagata, M., Weiner, J. A. & Sanes, J. R. Sidekicks: synaptic adhesion molecules that promote lamina-specific connectivity in the retina. Cell 110, 649–660 (2002). · DOI
  86. Wright, G. J., Martin, S., Bushell, K. M. & Sollner, C. High-throughput identification of transient extracellular protein interactions. Biochem. Soc. Trans. 38, 919–922 (2010). · DOI
  87. Wojtowicz, W. M. et al. A vast repertoire of Dscam binding specificities arises from modular interactions of variable Ig domains. Cell 130, 1134–1145 (2007). Wojtowicz and colleagues were the first to develop a high-throughput ELISA-based assay that allowed testing of the extracellular interaction specificity of a large number of Dscam1 isoforms. · DOI
  88. Bushell, K. M., Sollner, C., Schuster-Boeckler, B., Bateman, A. & Wright, G. J. Large-scale screening for novel low-affinity extracellular protein interactions. Genome Res. 18, 622–630 (2008). · DOI
  89. Ozkan, E. et al. An extracellular interactome of immunoglobulin and LRR proteins reveals receptor-ligand networks. Cell 154, 228–239 (2013). This large-scale extracellular interactome study tests the interactions of the complete extracellular D. melanogaster LRR, Ig superfamily and FN3 proteome (which corresponds to more than 20,000 unique pairwise interactions) and identifies close to 100 novel interactions, then validates them in fly embryos. · DOI
  90. Sollner, C. & Wright, G. J. A cell surface interaction network of neural leucine-rich repeat receptors. Genome Biol. 10, R99 (2009). · DOI
  91. Martin, S. et al. Construction of a large extracellular protein interaction network and its resolution by spatiotemporal expression profiling. Mol. Cell. Proteomics 9, 2654–2665 (2010). · DOI
  92. Kurusu, M. et al. A screen of cell-surface molecules identifies leucine-rich repeat proteins as key mediators of synaptic target selection. Neuron 59, 972–985 (2008). · DOI
  93. Zipursky, S. L. & Grueber, W. B. The molecular basis of self-avoidance. Annu. Rev. Neurosci. 36, 547–568 (2013). · DOI
  94. Lefebvre, J. L., Kostadinov, D., Chen, W. V., Maniatis, T. & Sanes, J. R. Protocadherins mediate dendritic self-avoidance in the mammalian nervous system. Nature 488, 517–521 (2012). This study shows that deletion of the γ-protocadherin cluster in retinal SACs and cerebellar Purkinje cells disrupts self-avoidance of their dendrites, indicating that protocadherin diversity provides these cell types with distinct surface identities required for proper establishment of their dendritic arbors. · DOI
  95. Garrett, A. M., Schreiner, D., Lobas, M. A. & Weiner, J. A. γ-protocadherins control cortical dendrite arborization by regulating the activity of a FAK/PKC/MARCKS signaling pathway. Neuron 74, 269–276 (2012). · DOI · Paper page
  96. Kay, J. N., Chu, M. W. & Sanes, J. R. MEGF10 and MEGF11 mediate homotypic interactions required for mosaic spacing of retinal neurons. Nature 483, 465–469 (2012). · DOI
  97. Sun, L. O. et al. On and off retinal circuit assembly by divergent molecular mechanisms. Science 342, 1241974 (2013). · DOI
  98. Gibson, D. A. et al. Dendrite self-avoidance requires cell-autonomous slit/robo signaling in cerebellar purkinje cells. Neuron 81, 1040–1056 (2014). · DOI
  99. Weiner, J. A., Wang, X., Tapia, J. C. & Sanes, J. R. Gamma protocadherins are required for synaptic development in the spinal cord. Proc. Natl Acad. Sci. USA 102, 8–14 (2005). · DOI
  100. Inoue, A. & Sanes, J. R. Lamina-specific connectivity in the brain: regulation by N-cadherin, neurotrophins, and glycoconjugates. Science 276, 1428–1431 (1997). · DOI
  101. Poskanzer, K., Needleman, L. A., Bozdagi, O. & Huntley, G. W. N-cadherin regulates ingrowth and laminar targeting of thalamocortical axons. J. Neurosci. 23, 2294–2305 (2003). · DOI
  102. Duan, X., Krishnaswamy, A., De la Huerta, I. & Sanes, J. R. Type II cadherins guide assembly of a direction-selective retinal circuit. Cell 158, 793–807 (2014). This article shows that the type II cadherins CDH8 and CDH9 are selectively expressed in distinct retinal cell types and instruct the targeting of the axons of these cells to specific sublaminae in the IPL of the mouse retina in vivo. · DOI
  103. Williams, M. E. et al. Cadherin-9 regulates synapse-specific differentiation in the developing hippocampus. Neuron 71, 640–655 (2011). This study uses a combination of in vitro assays and in vivo analysis to show that the type II cadherin CDH9 regulates specific connectivity between DG granule cell axons and CA3 pyramidal neurons in dissociated cultures and in the developing hippocampus. · DOI
  104. Bekirov, I. H., Nagy, V., Svoronos, A., Huntley, G. W. & Benson, D. L. Cadherin-8 and N-cadherin differentially regulate pre- and postsynaptic development of the hippocampal mossy fiber pathway. Hippocampus 18, 349–363 (2008). · DOI
  105. Ango, F. et al. Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at Purkinje axon initial segment. Cell 119, 257–272 (2004). This classic study demonstrates that the Ig superfamily protein neurofascin, which is expressed in a gradient on the Purkinje cell body and concentrates at the Purkinje axon initial segment, directs the subcellular specific innervation of the axon initial segment by GABAergic basket cell axons. · DOI
  106. Ashrafi, S. et al. Neuronal Ig/Caspr recognition promotes the formation of axoaxonic synapses in mouse spinal cord. Neuron 81, 120–129 (2014). This article shows that combinations of Ig superfamily proteins expressed on GABApre axons heterophilically interact with Ig superfamily proteins expressed on proprioceptive sensory axon terminals to promote the strikingly specific accumulation of GABApre synapses on sensory terminals in the spinal cord. · DOI
  107. Nishimura-Akiyoshi, S., Niimi, K., Nakashiba, T. & Itohara, S. Axonal netrin-Gs transneuronally determine lamina-specific subdendritic segments. Proc. Natl Acad. Sci. USA 104, 14801–14806 (2007). · DOI · Paper page
  108. DeNardo, L. A., de Wit, J., Otto-Hitt, S. & Ghosh, A. NGL-2 regulates input-specific synapse development in CA1 pyramidal neurons. Neuron 76, 762–775 (2012). · DOI
  109. Matsukawa, H. et al. Netrin-G/NGL complexes encode functional synaptic diversification. J. Neurosci. 34, 15779–15792 (2014). · DOI
  110. Aoto, J., Martinelli, D. C., Malenka, R. C., Tabuchi, K. & Sudhof, T. C. Presynaptic neurexin-3 alternative splicing trans-synaptically controls postsynaptic AMPA receptor trafficking. Cell 154, 75–88 (2013). This study uses a genetic approach to test the consequences of neurexin alternative splicing in vivo and finds that constitutive inclusion of a key splice site in neurexin decreases postsynaptic AMPAR levels, showing that neurexin alternative splicing trans -synaptically regulates glutamate receptor trafficking. · DOI
  111. Koester, H. J. & Johnston, D. Target cell-dependent normalization of transmitter release at neocortical synapses. Science 308, 863–866 (2005). · DOI
  112. Shigemoto, R. et al. Target-cell-specific concentration of a metabotropic glutamate receptor in the presynaptic active zone. Nature 381, 523–525 (1996). · DOI · Paper page
  113. Baier, H. Synaptic laminae in the visual system: molecular mechanisms forming layers of perception. Annu. Rev. Cell Dev. Biol. 29, 385–416 (2013). · DOI
  114. Robles, E. & Baier, H. Assembly of synaptic laminae by axon guidance molecules. Curr. Opin. Neurobiol. 22, 799–804 (2012). · DOI
  115. Reichelt, A. C., Rodgers, R. J. & Clapcote, S. J. The role of neurexins in schizophrenia and autistic spectrum disorder. Neuropharmacology 62, 1519–1526 (2012). · DOI
  116. Redies, C., Hertel, N. & Hubner, C. A. Cadherins and neuropsychiatric disorders. Brain Res. 1470, 130–144 (2012). · DOI
  117. Chen, J., Yu, S., Fu, Y. & Li, X. Synaptic proteins and receptors defects in autism spectrum disorders. Front. Cell Neurosci. 8, 276 (2014).
  118. Pasterkamp, R. J. Getting neural circuits into shape with semaphorins. Nat. Rev. Neurosci. 13, 605–618 (2012). · DOI
  119. Matsuoka, R. L. et al. Transmembrane semaphorin signalling controls laminar stratification in the mammalian retina. Nature 470, 259–263 (2011). · DOI
  120. Tawarayama, H., Yoshida, Y., Suto, F., Mitchell, K. J. & Fujisawa, H. Roles of semaphorin-6B and plexin-A2 in lamina-restricted projection of hippocampal mossy fibers. J. Neurosci. 30, 7049–7060 (2010). · DOI
  121. Suto, F. et al. Interactions between plexin-A2, plexin-A4, and semaphorin 6A control lamina-restricted projection of hippocampal mossy fibers. Neuron 53, 535–547 (2007). · DOI
  122. Hong, W., Mosca, T. J. & Luo, L. Teneurins instruct synaptic partner matching in an olfactory map. Nature 484, 201–207 (2012). · DOI
  123. Antinucci, P., Nikolaou, N., Meyer, M. P. & Hindges, R. Teneurin-3 specifies morphological and functional connectivity of retinal ganglion cells in the vertebrate visual system. Cell Rep. 5, 582–592 (2013). · DOI
  124. Biederer, T. et al. SynCAM, a synaptic adhesion molecule that drives synapse assembly. Science 297, 1525–1531 (2002). · DOI
  125. Fogel, A. I. et al. SynCAMs organize synapses through heterophilic adhesion. J. Neurosci. 27, 12516–12530 (2007). · DOI
  126. Robbins, E. M. et al. SynCAM 1 adhesion dynamically regulates synapse number and impacts plasticity and learning. Neuron 68, 894–906 (2010). · DOI
  127. Harwell, C. C. et al. Sonic hedgehog expression in corticofugal projection neurons directs cortical microcircuit formation. Neuron 73, 1116–1126 (2012). · DOI
  128. Kakegawa, W. et al. Anterograde C1ql1 signaling is required in order to determine and maintain a single-winner climbing fiber in the mouse cerebellum. Neuron 85, 316–329 (2015). · DOI
  129. Kalinovsky, A. et al. Development of axon-target specificity of ponto-cerebellar afferents. PLoS Biol. 9, e1001013 (2011). · DOI
  130. Pecho-Vrieseling, E., Sigrist, M., Yoshida, Y., Jessell, T. M. & Arber, S. Specificity of sensory-motor connections encoded by Sema3e–Plxnd1 recognition. Nature 459, 842–846 (2009). · DOI
  131. Kay, J. N. et al. Retinal ganglion cells with distinct directional preferences differ in molecular identity, structure, and central projections. J. Neurosci. 31, 7753–7762 (2011). · DOI
  132. Deguchi, Y., Donato, F., Galimberti, I., Cabuy, E. & Caroni, P. Temporally matched subpopulations of selectively interconnected principal neurons in the hippocampus. Nat. Neurosci. 14, 495–504 (2011). · DOI
  133. Kay, J. N., Voinescu, P. E., Chu, M. W. & Sanes, J. R. Neurod6 expression defines new retinal amacrine cell subtypes and regulates their fate. Nat. Neurosci. 14, 965–972 (2011). · DOI
  134. Arlotta, P. et al. Neuronal subtype-specific genes that control corticospinal motor neuron development in vivo. Neuron 45, 207–221 (2005). · DOI
  135. Ekstrand, M. I. et al. Molecular profiling of neurons based on connectivity. Cell 157, 1230–1242 (2014). · DOI
  136. Schwenk, J. et al. Regional diversity and developmental dynamics of the AMPA-receptor proteome in the mammalian brain. Neuron 84, 41–54 (2014). · DOI
  137. Schwenk, J. et al. High-resolution proteomics unravel architecture and molecular diversity of native AMPA receptor complexes. Neuron 74, 621–633 (2012). · DOI · Paper page
  138. Savas, J. N. et al. Ecto-Fc MS identifies ligand-receptor interactions through extracellular domain Fc fusion protein baits and shotgun proteomic analysis. Nat. Protoc. 9, 2061–2074 (2014). · DOI

Cited by

See all 242

Metadata

Authors
de Wit, J., & Ghosh, A.
Venue
Nature Reviews Neuroscience
Published
2015-12-10
Volume
17
Issue
1
Pages
4-4
ISSN
  • 1471-003X
  • 1471-0048
Cited by
242
References
24
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.