References
- Ammendrup-Johnsen, I., Naito, Y., Craig, A.M., and Takahashi, H. (2015). Neurotrophin-3 enhances the synaptic organizing function of TrkC-protein tyrosine phosphatase sigma in rat hippocampal neurons. J. Neurosci. 35, 12425-12431. https://doi.org/10.1523/JNEUROSCI.1330-15.2015
- Aricescu, A.R., McKinnell, I.W., Halfter, W., and Stoker, A.W. (2002). Heparan sulfate proteoglycans are ligands for receptor protein tyrosine phosphatase sigma. Mol. Cell Biol. 22, 1881-1892. https://doi.org/10.1128/MCB.22.6.1881-1892.2002
- Aruga, J., and Mikoshiba, K. (2003). Identification and characterization of Slitrk, a novel neuronal transmembrane protein family controlling neurite outgrowth. Mol. Cell. Neurosci. 24, 117-129. https://doi.org/10.1016/S1044-7431(03)00129-5
- Aruga, J., Yokota, N., and Mikoshiba, K. (2003). Human SLITRK family genes: genomic organization and expression profiling in normal brain and brain tumor tissue. Gene 315, 87-94. https://doi.org/10.1016/S0378-1119(03)00715-7
- Banfield, M.J., Naylor, R.L., Robertson, A.G., Allen, S.J., Dawbarn, D., and Brady, R.L. (2001). Specificity in Trk receptor:neurotrophin interactions: the crystal structure of TrkB-d5 in complex with neurotrophin-4/5. Structure 9, 1191-1199. https://doi.org/10.1016/S0969-2126(01)00681-5
- Barbacid, M. (1994). The Trk family of neurotrophin receptors. J. Neurobiol. 25, 1386-1403. https://doi.org/10.1002/neu.480251107
- Carrie, A., Jun, L., Bienvenu, T., Vinet, M.C., McDonell, N., Couvert, P., Zemni, R., Cardona, A., Van Buggenhout, G., Frints, S., et al. (1999). A new member of the IL-1 receptor family highly expressed in hippocampus and involved in X-linked mental retardation. Nat. Genet. 23, 25-31.
- Choi, Y., Nam, J., Whitcomb, D.J., Song, Y.S., Kim, D., Jeon, S., Um, J.W., Lee, S.G., Woo, J., Kwon, S.K., et al. (2016). SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development. Sci. Rep. 6, 26676. https://doi.org/10.1038/srep26676
- Coles, C.H., Jones, E.Y., and Aricescu, A.R. (2015). Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses. Semin. Cell Dev. Biol. 37, 98-107. https://doi.org/10.1016/j.semcdb.2014.09.007
- Coles, C.H., Mitakidis, N., Zhang, P., Elegheert, J., Lu, W., Stoker, A.W., Nakagawa, T., Craig, A.M., Jones, E.Y., and Aricescu, A.R. (2014). Structural basis for extracellular cis and trans RPTPsigma signal competition in synaptogenesis. Nat. Commun. 5, 5209. https://doi.org/10.1038/ncomms6209
- Coles, C.H., Shen, Y., Tenney, A.P., Siebold, C., Sutton, G.C., Lu, W., Gallagher, J.T., Jones, E.Y., Flanagan, J.G., and Aricescu, A.R. (2011). Proteoglycan-specific molecular switch for RPTPsigma clustering and neuronal extension. Science 332, 484-488. https://doi.org/10.1126/science.1200840
- Dean, C., Scholl, F.G., Choih, J., DeMaria, S., Berger, J., Isacoff, E., and Scheiffele, P. (2003). Neurexin mediates the assembly of presynaptic terminals. Nat. Neurosci. 6, 708-716. https://doi.org/10.1038/nn1074
- Fogel, A.I., Stagi, M., Perez de Arce, K., and Biederer, T. (2011). Lateral assembly of the immunoglobulin protein SynCAM 1 controls its adhesive function and instructs synapse formation. EMBO J. 30, 4728-4738. https://doi.org/10.1038/emboj.2011.336
- Friedman, W.J. (2001). Cytokines regulate expression of the type 1 interleukin-1 receptor in rat hippocampal neurons and glia. Exp. Neurol. 168, 23-31. https://doi.org/10.1006/exnr.2000.7595
- Goto-Ito, S., Yamagata, A., Sato, Y., Uemura, T., Shiroshima, T., Maeda, A., Imai, A., Mori, H., Yoshida, T., and Fukai, S. (2018). Structural basis of trans-synaptic interactions between PTPdelta and SALMs for inducing synapse formation. Nat. Commun. 9, 269. https://doi.org/10.1038/s41467-017-02417-z
- Han, K.A., Jeon, S., Um, J.W., and Ko, J. (2016a). Emergent synapse organizers: LAR-RPTPs and their companions. Int. Rev. Cell Mol. Biol. 324, 39-65.
- Han, K.A., Woo, D., Kim, S., Choii, G., Jeon, S., Won, S.Y., Kim, H.M., Heo, W.D., Um, J.W., and Ko, J. (2016b). Neurotrophin-3 Regulates Synapse Development by Modulating TrkC-PTPsigma Synaptic Adhesion and Intracellular Signaling Pathways. J Neurosci 36, 4816-4831. https://doi.org/10.1523/JNEUROSCI.4024-15.2016
- Harrison, O.J., Jin, X., Hong, S., Bahna, F., Ahlsen, G., Brasch, J., Wu, Y., Vendome, J., Felsovalyi, K., Hampton, C.M., et al. (2011). The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins. Structure 19, 244-256. https://doi.org/10.1016/j.str.2010.11.016
- Himanen, J.P., Yermekbayeva, L., Janes, P.W., Walker, J.R., Xu, K., Atapattu, L., Rajashankar, K.R., Mensinga, A., Lackmann, M., Nikolov, D.B., et al. (2010). Architecture of Eph receptor clusters. Proc. Natl. Acad. Sci. USA 107, 10860-10865. https://doi.org/10.1073/pnas.1004148107
- Kang, H., Han, K.A., Won, S.Y., Kim, H.M., Lee, Y.H., Ko, J., and Um, J.W. (2016). Slitrk missense mutations associated with neuropsychiatric disorders distinctively impair slitrk trafficking and synapse formation. Front. Mol. Neurosci. 9, 104.
- Ko, J. (2012). The leucine-rich repeat superfamily of synaptic adhesion molecules: LRRTMs and Slitrks. Mol. Cells 34, 335-340. https://doi.org/10.1007/s10059-012-0113-3
- Ko, J.S., Pramanik, G., Um, J.W., Shim, J.S., Lee, D., Kim, K.H., Chung, G.Y., Condomitti, G., Kim, H.M., Kim, H., et al. (2015). PTPsigma functions as a presynaptic receptor for the glypican-4/LRRTM4 complex and is essential for excitatory synaptic transmission. Proc. Natl. Acad. Sci. USA 112, 1874-1879. https://doi.org/10.1073/pnas.1410138112
- Li, Y., Zhang, P., Choi, T.Y., Park, S.K., Park, H., Lee, E.J., Lee, D., Roh, J.D., Mah, W., Kim, R., et al. (2015). Splicing-dependent trans-synaptic SALM3-LAR-RPTP interactions regulate excitatory synapse development and locomotion. Cell Rep. 12, 1618-1630. https://doi.org/10.1016/j.celrep.2015.08.002
- Lie, E., Li, Y., Kim, R., and Kim, E. (2018). SALM/Lrfn family synaptic adhesion molecules. Front Mol. Neurosci. 11, 105. https://doi.org/10.3389/fnmol.2018.00105
- Lin, Z., Liu, J., Ding, H., Xu, F., and Liu, H. (2018). Structural basis of SALM5-induced PTPdelta dimerization for synaptic differentiation. Nat. Commun. 9, 268. https://doi.org/10.1038/s41467-017-02414-2
- Mah, W., Ko, J., Nam, J., Han, K., Chung, W.S., and Kim, E. (2010). Selected SALM (synaptic adhesion-like molecule) family proteins regulate synapse formation. J. Neurosci. 30, 5559-5568. https://doi.org/10.1523/JNEUROSCI.4839-09.2010
- Nam, H.J., Poy, F., Krueger, N.X., Saito, H., and Frederick, C.A. (1999). Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell 97, 449-457. https://doi.org/10.1016/S0092-8674(00)80755-2
- Park, B.S., Song, D.H., Kim, H.M., Choi, B.S., Lee, H., and Lee, J.O. (2009). The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458, 1191-U1130. https://doi.org/10.1038/nature07830
- Piton, A., Michaud, J.L., Peng, H., Aradhya, S., Gauthier, J., Mottron, L., Champagne, N., Lafreniere, R.G., Hamdan, F.F., team, S.D., et al. (2008). Mutations in the calcium-related gene IL1RAPL1 are associated with autism. Hum. Mol. Genet. 17, 3965-3974. https://doi.org/10.1093/hmg/ddn300
- Pulido, R., Serra-Pages, C., Tang, M., and Streuli, M. (1995). The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. Proc. Natl. Acad. Sci. USA 92, 11686-11690. https://doi.org/10.1073/pnas.92.25.11686
- Seiradake, E., Harlos, K., Sutton, G., Aricescu, A.R., and Jones, E.Y. (2010). An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly. Nat Struct Mol Biol 17, 398-402. https://doi.org/10.1038/nsmb.1782
- Shaftel, S.S., Griffin, W.S., and O'Banion, M.K. (2008). The role of interleukin-1 in neuroinflammation and Alzheimer disease: an evolving perspective. J. Neuroinflammation 5, 7. https://doi.org/10.1186/1742-2094-5-7
- Shen, Y., Tenney, A.P., Busch, S.A., Horn, K.P., Cuascut, F.X., Liu, K., He, Z., Silver, J., and Flanagan, J.G. (2009). PTPsigma is a receptor for chondroitin sulfate proteoglycan, an inhibitor of neural regeneration. Science 326, 592-596. https://doi.org/10.1126/science.1178310
- Sims, J.E., and Smith, D.E. (2010). The IL-1 family: regulators of immunity. Nat. Rev. Immunol. 10, 89-102. https://doi.org/10.1038/nri2691
- Takahashi, H., and Craig, A.M. (2013). Protein tyrosine phosphatases PTPdelta, PTPsigma, and LAR: presynaptic hubs for synapse organization. Trends Neurosci. 36, 522-534. https://doi.org/10.1016/j.tins.2013.06.002
- Takahashi, H., Arstikaitis, P., Prasad, T., Bartlett, T.E., Wang, Y.T., Murphy, T.H., and Craig, A.M. (2011). Postsynaptic TrkC and presynaptic PTPsigma function as a bidirectional excitatory synaptic organizing complex. Neuron 69, 287-303. https://doi.org/10.1016/j.neuron.2010.12.024
- Takahashi, H., Katayama, K., Sohya, K., Miyamoto, H., Prasad, T., Matsumoto, Y., Ota, M., Yasuda, H., Tsumoto, T., Aruga, J., et al. (2012). Selective control of inhibitory synapse development by Slitrk3-PTPdelta trans-synaptic interaction. Nat. Neurosci. 15, 389-398, S381-382. https://doi.org/10.1038/nn.3040
- Tanaka, H., Miyazaki, N., Matoba, K., Nogi, T., Iwasaki, K., and Takagi, J. (2012). Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin. Cell Rep. 2, 101-110. https://doi.org/10.1016/j.celrep.2012.06.009
- Thomas, C., Bazan, J.F., and Garcia, K.C. (2012). Structure of the activating IL-1 receptor signaling complex. Nat. Struct. Mol. Biol. 19, 455-457. https://doi.org/10.1038/nsmb.2260
- Tonks, N.K. (2006). Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 7, 833-846.
- Um, J.W., Kim, K.H., Park, B.S., Choi, Y., Kim, D., Kim, C.Y., Kim, S.J., Kim, M., Ko, J.S., Lee, S.G., et al. (2014). Structural basis for LAR-RPTP/Slitrk complex-mediated synaptic adhesion. Nat. Commun. 5, 5423. https://doi.org/10.1038/ncomms6423
- Um, J.W., and Ko, J. (2013). LAR-RPTPs: synaptic adhesion molecules that shape synapse development. Trends Cell Biol. 23, 465-475. https://doi.org/10.1016/j.tcb.2013.07.004
- Valnegri, P., Montrasio, C., Brambilla, D., Ko, J., Passafaro, M., and Sala, C. (2011). The X-linked intellectual disability protein IL1RAPL1 regulates excitatory synapse formation by binding PTPdelta and RhoGAP2. Hum. Mol. Genet. 20, 4797-4809. https://doi.org/10.1093/hmg/ddr418
- Wallace, M.J., Fladd, C., Batt, J., and Rotin, D. (1998). The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma. Mol. Cell Biol. 18, 2608-2616. https://doi.org/10.1128/MCB.18.5.2608
- Wang, D., Zhang, S., Li, L., Liu, X., Mei, K., and Wang, X. (2010). Structural insights into the assembly and activation of IL-1beta with its receptors. Nat. Immunol. 11, 905-911. https://doi.org/10.1038/ni.1925
- Wiesmann, C., Ultsch, M.H., Bass, S.H., and de Vos, A.M. (1999). Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Nature 401, 184-188. https://doi.org/10.1038/43705
- Won, S.Y., Kim, C.Y., Kim, D., Ko, J., Um, J.W., Lee, S.B., Buck, M., Kim, E., Heo, W.D., Lee, J.O., et al. (2017). LAR-RPTP clustering is modulated by competitive binding between synaptic adhesion partners and heparan sulfate. Front. Mol. Neurosci. 10, 327. https://doi.org/10.3389/fnmol.2017.00327
- Woo, J., Kwon, S.K., Choi, S., Kim, S., Lee, J.R., Dunah, A.W., Sheng, M., and Kim, E. (2009). Trans-synaptic adhesion between NGL-3 and LAR regulates the formation of excitatory synapses. Nat. Neurosci. 12, 428-437. https://doi.org/10.1038/nn.2279
- Xu, Y., and Fisher, G.J. (2012). Receptor type protein tyrosine phosphatases (RPTPs) - roles in signal transduction and human disease. J Cell Commun Signal 6, 125-138. https://doi.org/10.1007/s12079-012-0171-5
- Yamagata, A., Sato, Y., Goto-Ito, S., Uemura, T., Maeda, A., Shiroshima, T., Yoshida, T., and Fukai, S. (2015a). Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing-dependent transsynaptic adhesion. Sci. Rep. 5, 9686. https://doi.org/10.1038/srep09686
- Yamagata, A., Yoshida, T., Sato, Y., Goto-Ito, S., Uemura, T., Maeda, A., Shiroshima, T., Iwasawa-Okamoto, S., Mori, H., Mishina, M., et al. (2015b). Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-IL1RAPL1/IL-1RAcP for synaptic differentiation. Nat. Commun. 6, 6926. https://doi.org/10.1038/ncomms7926
- Yim, Y.S., Kwon, Y., Nam, J., Yoon, H.I., Lee, K., Kim, D.G., Kim, E., Kim, C.H., and Ko, J. (2013). Slitrks control excitatory and inhibitory synapse formation with LAR receptor protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 110, 4057-4062. https://doi.org/10.1073/pnas.1209881110
- Yoshida, T., Yasumura, M., Uemura, T., Lee, S.J., Ra, M., Taguchi, R., Iwakura, Y., and Mishina, M. (2011). IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase delta. J. Neurosci. 31, 13485-13499. https://doi.org/10.1523/JNEUROSCI.2136-11.2011
- Yoshida, T., Shiroshima, T., Lee, S.J., Yasumura, M., Uemura, T., Chen, X., Iwakura, Y., and Mishina, M. (2012). Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule. J. Neurosci. 32, 2588-2600. https://doi.org/10.1523/JNEUROSCI.4637-11.2012
Cited by
- LAR receptor phospho-tyrosine phosphatases regulate NMDA-receptor responses vol.9, pp.None, 2018, https://doi.org/10.7554/elife.53406
- LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain vol.9, pp.None, 2018, https://doi.org/10.3389/fcell.2021.659951
- The CNS/PNS Extracellular Matrix Provides Instructive Guidance Cues to Neural Cells and Neuroregulatory Proteins in Neural Development and Repair vol.22, pp.11, 2018, https://doi.org/10.3390/ijms22115583