Structure of Slitrk2-PTP complex reveals mechanisms for splicing-dependent trans-synaptic adhesion

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Yamagata, Atsushi ^a   Sato, Yusuke ^b   Goto Ito, Sakurako ^c   Uemura, Takeshi ^d   Maeda, Asami ^e   Shiroshima, Tomoko ^f   Yoshida, Tomoyuki ^c   Fukai, Shuya ^a  

^a Institute of Molecular and Cellular Biosciences   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d SHINSHU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^e SHINSHU UNIVERSITY   (Japan)

^f UNIVERSITY OF TOYAMA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

LRR1 PROTEIN, HUMAN; PROTEIN BINDING; PTPRD PROTEIN, MOUSE; RECEPTOR LIKE PROTEIN TYROSINE PHOSPHATASE; REPRESSOR PROTEIN;

ANIMAL; BINDING SITE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR MODEL; MOUSE; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION; SYNAPSE;

ANIMALS; BINDING SITES; HUMANS; MICE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; RECEPTOR-LIKE PROTEIN TYROSINE PHOSPHATASES, CLASS 2; REPRESSOR PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SYNAPSES;

EID: 84930221725     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep09686     Document Type: Article

References (24)

1. Takahashi, H. &Craig, A. M. Protein tyrosine phosphatases PTPd, PTPs, and LAR: presynaptic hubs for synapse organization. Trends Neurosci. 36, 522-534 (2013
2. Um, J. W. &Ko, J. LAR-RPTPs: synaptic adhesion molecules that shape synapse development. Trends Cell Biol. 23, 465-475 (2013
3. Yoshida, T. et al. Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule. J. Neurosci. 32, 2588-2600 (2012
4. Yoshida, T. et al. IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase d. J. Neurosci. 31, 13485-13499 (2011
5. Woo, J. et al. Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses. Nat. Neurosci. 12, 428-437 (2009
6. Takahashi, H. et al. Postsynaptic TrkC and presynaptic PTPs function as a bidirectional excitatory synaptic organizing complex. Neuron 69, 287-303 (2011
7. Takahashi, H. et al. Selective control of inhibitory synapse development by Slitrk3-PTPdelta trans-synaptic interaction. Nat. Neurosci. 15, 389-398 (2012
8. Yim, Y. S. et al. Slitrks control excitatory and inhibitory synapse formation with LAR receptor protein tyrosine phosphatases. Proc. Natl. Acad. Sci. U. S. A. 110, 4057-4062 (2013
9. Aruga, J. &Mikoshiba, K. Identification and characterization of Slitrk, a novel neuronal transmembrane protein family controlling neurite outgrowth. Mol. Cell. Neurosci. 24, 117-129 (2003
10. Proenca, C. C., Gao, K. P., Shmelkov, S. V., Rafii, S. &Lee, F. S. Slitrks as emerging candidate genes involved in neuropsychiatric disorders. Trends Neurosci. 34, 143-153 (2011
11. Abelson, J. F. et al. Sequence variants in SLITRK1 are associated with Tourette's syndrome. Science 310, 317-320 (2005
12. Zuchner, S. et al. SLITRK1 mutations in trichotillomania. Mol. Psychiatry 11, 887-889 (2006
13. Piton, A. et al. Systematic resequencing of X-chromosome synaptic genes in autism spectrum disorder and schizophrenia. Mol. Psychiatry 16, 867-880 (2011
14. Smith, E. N. et al. Genome-wide association of bipolar disorder suggests an enrichment of replicable associations in regions near genes. PLoS Genet. 7, e1002134 (2011
15. Coles, C. H. et al. Proteoglycan-specific molecular switch for RPTPs clustering and neuronal extension. Science 332, 484-488 (2011
16. He, X. L. et al. Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. Neuron 38, 177-185 (2003
17. Um, J. M. et al. Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion. Nat. Commun. 5, 5423 (2014
18. Aricescu, A.R., Lu, W. &Jones, E.Y. A time-And cost-efficient systemfor high-level protein production in mammalian cells. Acta. Crystallogr. D 62, 1243-50 (2006
19. Otwinowski, Z. &Minor, W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods Enzymol. 276, 20 (1997
20. Vagin, A. &Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 4 (1997
21. Emsley, P. &Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132 (2004
22. Adams, P. D. et al. The Phenix software for automated determination of macromolecular structures. Methods 55, 94-106 (2011
23. Laskowski, R. A., Macarthur, M. W., Moss, D. S. &Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 9 (1993
24. Krissinel, E. &Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007