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VPS10P Domain Receptors: Sorting Out Brain Health and Disease

Malik, Anna R., Willnow, Thomas E.·2020·Trends in Neurosciences
DOI 10.1016/j.tins.2020.08.003
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Abstract

VPS10P (vacuolar protein sorting 10 protein) domain receptors are neuronal sorting receptors that direct cargo proteins to their destined location in subcellular compartments of the soma, dendrites, and the axon. Protein sorting by receptors such as SORLA, sortilin, and SorCS2 controls functional integrity and viability of neurons, whereas sorting receptor dysfunctions are linked to acute, psychiatric, and neurodegenerative diseases. Here, we discuss molecular mechanisms that define ligand repertoire and sorting path and that control plasticity of VPS10P domain receptor expression in the healthy brain and in response to injury. These findings highlight important concepts in neuronal protein sorting and why aberrant sorting contributes to the progression of devastating diseases of the human brain, including epilepsy, Alzheimer's disease, and frontotemporal dementia.

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  1. Leloup, 2018, Structural insights into SorCS2-nerve growth factor complex formation, Nat. Commun., 9, 2979, 10.1038/s41467-018-05405-z · DOI
  2. Quistgaard, 2014, Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin, Protein Sci., 23, 1291, 10.1002/pro.2512 · DOI
  3. Dumanis, 2015, Distinct functions for anterograde and retrograde sorting of SORLA in amyloidogenic processes in the brain, J. Neurosci., 35, 12703, 10.1523/JNEUROSCI.0427-15.2015 · DOI
  4. Vaegter, 2011, Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling, Nat. Neurosci., 14, 54, 10.1038/nn.2689 · DOI
  5. Glerup, 2016, SorCS2 is required for BDNF-dependent plasticity in the hippocampus, Mol. Psychiatry, 21, 1740, 10.1038/mp.2016.108 · DOI
  6. Yang, 2011, Precursor of brain-derived neurotrophic factor (proBDNF) forms a complex with Huntingtin-associated protein-1 (HAP1) and sortilin that modulates proBDNF trafficking, degradation, and processing, J. Biol. Chem., 286, 16272, 10.1074/jbc.M110.195347 · DOI
  7. Jansen, 2007, Roles for the pro-neurotrophin receptor sortilin in neuronal development, aging and brain injury, Nat. Neurosci., 10, 1449, 10.1038/nn2000 · DOI · Paper page
  8. Kim, 2009, NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death, EMBO J., 28, 1612, 10.1038/emboj.2009.118 · DOI
  9. Malik, 2020, SorCS2 facilitates release of endostatin from astrocytes and controls post-stroke angiogenesis, Glia, 68, 1304, 10.1002/glia.23778 · DOI
  10. Malik, 2019, SorCS2 controls functional expression of amino acid transporter EAAT3 and protects neurons from oxidative stress and epilepsy-induced pathology, Cell Rep., 26, 2792, 10.1016/j.celrep.2019.02.027 · DOI
  11. Lambert, 2013, Meta-analysis of 74,046 individuals identifies 11 new susceptibility loci for Alzheimer's disease, Nat. Genet., 45, 1452, 10.1038/ng.2802 · DOI · Paper page
  12. Pottier, 2012, High frequency of potentially pathogenic SORL1 mutations in autosomal dominant early-onset Alzheimer disease, Mol. Psychiatry, 17, 875, 10.1038/mp.2012.15 · DOI · Paper page
  13. Nicolas, 2015, SORL1 rare variants: a major risk factor for familial early-onset Alzheimer's disease, Mol. Psychiatry, 21, 831, 10.1038/mp.2015.121 · DOI · Paper page
  14. Verheijen, 2016, A comprehensive study of the genetic impact of rare variants in SORL1 in European early-onset Alzheimer's disease, Acta Neuropathol., 132, 213, 10.1007/s00401-016-1566-9 · DOI · Paper page
  15. Carrasquillo, 2010, Genome-wide screen identifies rs646776 near sortilin as a regulator of progranulin levels in human plasma, Am. J. Hum. Genet., 87, 890, 10.1016/j.ajhg.2010.11.002 · DOI · Paper page
  16. Breiderhoff, 2013, Sortilin-related receptor SORCS3 is a postsynaptic modulator of synaptic depression and fear extinction, PLoS One, 8, 10.1371/journal.pone.0075006 · DOI
  17. Yang, 2020, SorCS2 is required for social memory and trafficking of the NMDA receptor, Mol. Psychiatry
  18. Buttenschon, 2015, Increased serum levels of sortilin are associated with depression and correlated with BDNF and VEGF, Transl. Psychiatry, 5, e677, 10.1038/tp.2015.167 · DOI
  19. Andersen, 2005, Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein, Proc. Natl. Acad. Sci. U. S. A., 102, 13461, 10.1073/pnas.0503689102 · DOI · Paper page
  20. Caglayan, 2014, Lysosomal sorting of amyloid-beta by the SORLA receptor is impaired by a familial Alzheimer's disease mutation, Sci. Transl. Med., 6, 10.1126/scitranslmed.3007747 · DOI · Paper page
  21. Paiardini, 2008, Insights into the interaction of sortilin with proneurotrophins: a computational approach, Neuropeptides, 42, 205, 10.1016/j.npep.2007.11.004 · DOI
  22. Serup Andersen, 2010, Identification of a linear epitope in sortilin that partakes in pro-neurotrophin binding, J. Biol. Chem., 285, 12210, 10.1074/jbc.M109.062364 · DOI
  23. Chen, 2005, Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway, J. Neurosci., 25, 6156, 10.1523/JNEUROSCI.1017-05.2005 · DOI
  24. Rohe, 2013, SORLA-mediated trafficking of TrkB enhances the response of neurons to BDNF, PLoS One, 8, 10.1371/journal.pone.0072164 · DOI
  25. Subkhangulova, 2018, SORCS1 and SORCS3 control energy balance and orexigenic peptide production, EMBO Rep., 19, 10.15252/embr.201744810 · DOI
  26. Glerup, 2014, SorCS2 regulates dopaminergic wiring and is processed into an apoptotic two-chain receptor in peripheral glia, Neuron, 82, 1074, 10.1016/j.neuron.2014.04.022 · DOI
  27. Zanin, 2016, Proneurotrophin-3 promotes cell cycle withdrawal of developing cerebellar granule cell progenitors via the p75 neurotrophin receptor, Elife, 5, 10.7554/eLife.16654 · DOI
  28. Geng, 2011, Sorting protein-related receptor SorLA controls regulated secretion of glial cell line-derived neurotrophic factor, J. Biol. Chem., 286, 41871, 10.1074/jbc.M111.246413 · DOI
  29. Glerup, 2013, SorLA controls neurotrophic activity by sorting of GDNF and its receptors GFRalpha1 and RET, Cell Rep., 3, 186, 10.1016/j.celrep.2012.12.011 · DOI · Paper page
  30. Larsen, 2010, Sortilin facilitates signaling of ciliary neurotrophic factor and related helical type 1 cytokines targeting the gp130/leukemia inhibitory factor receptor beta heterodimer, Mol. Cell. Biol., 30, 4175, 10.1128/MCB.00274-10 · DOI
  31. Schroder, 2014, The identification of AF38469: an orally bioavailable inhibitor of the VPS10P family sorting receptor sortilin, Bioorg. Med. Chem. Lett., 24, 177, 10.1016/j.bmcl.2013.11.046 · DOI
  32. Andersen, 2014, Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex, Acta Crystallogr. D Biol. Crystallogr., 70, 451, 10.1107/S1399004713030149 · DOI
  33. Yang, 2019, Sortilin promotes glioblastoma invasion and mesenchymal transition through GSK-3beta/beta-catenin/twist pathway, Cell Death Dis., 10, 10.1038/s41419-019-1449-9 · DOI
  34. Ho, 2019, A novel peptide interfering with proBDNF-sortilin interaction alleviates chronic inflammatory pain, Theranostics, 9, 1651, 10.7150/thno.29703 · DOI
  35. Malik, 2018, Development of a cell-based assay to assess binding of the proNGF prodomain to sortilin, Cell. Mol. Neurobiol., 38, 827, 10.1007/s10571-017-0558-1 · DOI
  36. Lee, 2014, Targeted manipulation of the sortilin-progranulin axis rescues progranulin haploinsufficiency, Hum. Mol. Genet., 23, 1467, 10.1093/hmg/ddt534 · DOI · Paper page
  37. Quistgaard, 2009, Ligands bind to sortilin in the tunnel of a ten-bladed beta-propeller domain, Nat. Struct. Mol. Biol., 16, 96, 10.1038/nsmb.1543 · DOI
  38. Kitago, 2015, Structural basis for amyloidogenic peptide recognition by sorLA, Nat. Struct. Mol. Biol., 22, 199, 10.1038/nsmb.2954 · DOI · Paper page
  39. Januliene, 2017, Acidic environment induces dimerization and ligand binding site collapse in the Vps10p domain of sortilin, Structure, 25, 1809, 10.1016/j.str.2017.09.015 · DOI
  40. Leloup, 2017, Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release, Nat. Commun., 8, 10.1038/s41467-017-01485-5 · DOI
  41. Yabe-Wada, 2018, Crystal structure of the ligand-free form of the Vps10 ectodomain of dimerized sortilin at acidic pH, FEBS Lett., 592, 2647, 10.1002/1873-3468.13181 · DOI
  42. Itoh, 2018, Dimerization of sortilin regulates its trafficking to extracellular vesicles, J. Biol. Chem., 293, 4532, 10.1074/jbc.RA117.000732 · DOI
  43. Januliene, 2017, Hidden twins: SorCS neuroreceptors form stable dimers, J. Mol. Biol., 429, 2907, 10.1016/j.jmb.2017.08.006 · DOI
  44. Westergaard, 2004, Functional organization of the sortilin Vps10p domain, J. Biol. Chem., 279, 50221, 10.1074/jbc.M408873200 · DOI
  45. Westergaard, 2005, SorCS3 does not require propeptide cleavage to bind nerve growth factor, FEBS Lett., 579, 1172, 10.1016/j.febslet.2004.12.088 · DOI
  46. Mazella, 2010, Spadin, a sortilin-derived peptide, targeting rodent TREK-1 channels: a new concept in the antidepressant drug design, PLoS Biol., 8, 10.1371/journal.pbio.1000355 · DOI
  47. Hampe, 2000, Ectodomain shedding, translocation and synthesis of SorLA are stimulated by its ligand head activator, J. Cell Sci., 113, 4475, 10.1242/jcs.113.24.4475 · DOI · Paper page
  48. Herskowitz, 2011, Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production, J. Biol. Chem., 286, 6117, 10.1074/jbc.M110.167239 · DOI
  49. Tsukamoto, 2014, Tetraspanin CD9 modulates ADAM17-mediated shedding of LR11 in leukocytes, Exp. Mol. Med., 46, e89, 10.1038/emm.2013.161 · DOI
  50. Whittle, 2015, Soluble LR11/SorLA represses thermogenesis in adipose tissue and correlates with BMI in humans, Nat. Commun., 6, 8951, 10.1038/ncomms9951 · DOI
  51. Stupack, 2020, Soluble SORLA enhances neurite outgrowth and regeneration through activation of the EGF receptor/ERK signaling axis, J. Neurosci., 40, 5908, 10.1523/JNEUROSCI.0723-20.2020 · DOI
  52. Prudencio, 2012, Misregulation of human sortilin splicing leads to the generation of a nonfunctional progranulin receptor, Proc. Natl. Acad. Sci. U. S. A., 109, 21510, 10.1073/pnas.1211577110 · DOI
  53. Ma, 2009, Reduction of SorLA/LR11, a sorting protein limiting beta-amyloid production, in Alzheimer disease cerebrospinal fluid, Arch. Neurol., 66, 448, 10.1001/archneurol.2009.22 · DOI
  54. Hermey, 2003, Characterization of sorCS1, an alternatively spliced receptor with completely different cytoplasmic domains that mediate different trafficking in cells, J. Biol. Chem., 278, 7390, 10.1074/jbc.M210851200 · DOI
  55. Ribeiro, 2019, SorCS1-mediated sorting in dendrites maintains neurexin axonal surface polarization required for synaptic function, PLoS Biol., 17, 10.1371/journal.pbio.3000466 · DOI
  56. Hu, 2010, Sortilin-mediated endocytosis determines levels of the frontotemporal dementia protein, progranulin, Neuron, 68, 654, 10.1016/j.neuron.2010.09.034 · DOI · Paper page
  57. Pinet, 2016, TrkB-containing exosomes promote the transfer of glioblastoma aggressiveness to YKL-40-inactivated glioblastoma cells, Oncotarget, 7, 50349, 10.18632/oncotarget.10387 · DOI
  58. Selkoe, 2016, The amyloid hypothesis of Alzheimer's disease at 25 years, EMBO Mol. Med., 8, 595, 10.15252/emmm.201606210 · DOI · Paper page
  59. Rohe, 2008, Sortilin-related receptor with A-type repeats (SORLA) affects the amyloid precursor protein-dependent stimulation of ERK signaling and adult neurogenesis, J. Biol. Chem., 283, 14826, 10.1074/jbc.M710574200 · DOI · Paper page
  60. Burgert, 2013, SORLA-dependent and -independent functions for PACS1 in control of amyloidogenic processes, Mol. Cell. Biol., 33, 4308, 10.1128/MCB.00628-13 · DOI
  61. Fjorback, 2012, Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing, J. Neurosci., 32, 1467, 10.1523/JNEUROSCI.2272-11.2012 · DOI · Paper page
  62. Cuccaro, 2016, SORL1 mutations in early- and late-onset Alzheimer disease, Neurol. Genet., 2, e116, 10.1212/NXG.0000000000000116 · DOI · Paper page
  63. Vardarajan, 2012, Identification of Alzheimer disease-associated variants in genes that regulate retromer function, Neurobiol. Aging, 33, 2231, 10.1016/j.neurobiolaging.2012.04.020 · DOI · Paper page
  64. Finch, 2009, Plasma progranulin levels predict progranulin mutation status in frontotemporal dementia patients and asymptomatic family members, Brain, 132, 583, 10.1093/brain/awn352 · DOI
  65. Nicholson, 2014, Progranulin protein levels are differently regulated in plasma and CSF, Neurology, 82, 1871, 10.1212/WNL.0000000000000445 · DOI
  66. Molgaard, 2016, Soluble sortilin is present in excess and positively correlates with progranulin in CSF of aging individuals, Exp. Gerontol., 84, 96, 10.1016/j.exger.2016.09.002 · DOI
  67. Mohagheghi, 2016, TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor, Hum. Mol. Genet., 25, 534, 10.1093/hmg/ddv491 · DOI
  68. Beel, 2017, Progranulin functions as a cathepsin D chaperone to stimulate axonal outgrowth in vivo, Hum. Mol. Genet., 26, 2850, 10.1093/hmg/ddx162 · DOI · Paper page
  69. Butler, 2019, Progranulin stimulates the in vitro maturation of pro-cathepsin D at acidic pH, J. Mol. Biol., 431, 1038, 10.1016/j.jmb.2019.01.027 · DOI
  70. Nicholson, 2016, Prosaposin is a regulator of progranulin levels and oligomerization, Nat. Commun., 7, 10.1038/ncomms11992 · DOI · Paper page
  71. Zhou, 2017, Impaired prosaposin lysosomal trafficking in frontotemporal lobar degeneration due to progranulin mutations, Nat. Commun., 8, 10.1038/ncomms15277 · DOI
  72. Jacobsen, 1996, Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein, J. Biol. Chem., 271, 31379, 10.1074/jbc.271.49.31379 · DOI · Paper page
  73. Sarret, 2003, Distribution of NTS3 receptor/sortilin mRNA and protein in the rat central nervous system, J. Comp. Neurol., 461, 483, 10.1002/cne.10708 · DOI · Paper page
  74. Hermey, 2004, The three sorCS genes are differentially expressed and regulated by synaptic activity, J. Neurochem., 88, 1470, 10.1046/j.1471-4159.2004.02286.x · DOI
  75. Boggild, 2018, Highly segregated localization of the functionally related vps10p receptors sortilin and SorCS2 during neurodevelopment, J. Comp. Neurol., 526, 1267, 10.1002/cne.24403 · DOI
  76. Ma, 2007, Omega-3 fatty acid docosahexaenoic acid increases SorLA/LR11, a sorting protein with reduced expression in sporadic Alzheimer's disease (AD): relevance to AD prevention, J. Neurosci., 27, 14299, 10.1523/JNEUROSCI.3593-07.2007 · DOI
  77. Rohe, 2009, Brain-derived neurotrophic factor reduces amyloidogenic processing through control of SORLA gene expression, J. Neurosci., 29, 15472, 10.1523/JNEUROSCI.3960-09.2009 · DOI
  78. Young, 2015, Elucidating molecular phenotypes caused by the SORL1 Alzheimer's disease genetic risk factor using human induced pluripotent stem cells, Cell Stem Cell, 16, 373, 10.1016/j.stem.2015.02.004 · DOI
  79. Saadipour, 2013, Amyloid beta(1-42) (Abeta(42)) up-regulates the expression of sortilin via the p75(NTR)/RhoA signaling pathway, J. Neurochem., 127, 152, 10.1111/jnc.12383 · DOI
  80. Wei, 2007, Enhanced protein expressions of sortilin and p75NTR in retina of rat following elevated intraocular pressure-induced retinal ischemia, Neurosci. Lett., 429, 169, 10.1016/j.neulet.2007.10.012 · DOI
  81. Wang, 2010, Protective effects of octacosanol on 6-hydroxydopamine-induced Parkinsonism in rats via regulation of ProNGF and NGF signaling, Acta Pharmacol. Sin., 31, 765, 10.1038/aps.2010.69 · DOI
  82. Xu, 2009, Immunohistochemical localization of sortilin and p75(NTR) in normal and ischemic rat retina, Neurosci. Lett., 454, 81, 10.1016/j.neulet.2009.02.036 · DOI
  83. Hermey, 2009, The Vps10p-domain receptor family, Cell. Mol. Life Sci., 66, 2677, 10.1007/s00018-009-0043-1 · DOI
  84. Nielsen, 2007, Sorting by the cytoplasmic domain of the amyloid precursor protein binding receptor SorLA, Mol. Cell. Biol., 27, 6842, 10.1128/MCB.00815-07 · DOI · Paper page
  85. Klinger, 2016, Polarized trafficking of the sorting receptor SorLA in neurons and MDCK cells, FEBS J., 283, 2476, 10.1111/febs.13758 · DOI
  86. Canuel, 2008, AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes, Biochem. Biophys. Res. Commun., 366, 724, 10.1016/j.bbrc.2007.12.015 · DOI
  87. Baltes, 2014, Sigma1B adaptin regulates adipogenesis by mediating the sorting of sortilin in adipose tissue, J. Cell Sci., 127, 3477
  88. Schmidt, 2007, SorLA/LR11 regulates processing of amyloid precursor protein via interaction with adaptors GGA and PACS-1, J. Biol. Chem., 282, 32956, 10.1074/jbc.M705073200 · DOI · Paper page
  89. Jacobsen, 2002, The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding, FEBS Lett., 511, 155, 10.1016/S0014-5793(01)03299-9 · DOI
  90. Herskowitz, 2012, GGA1-mediated endocytic traffic of LR11/SorLA alters APP intracellular distribution and amyloid-beta production, Mol. Biol. Cell, 23, 2645, 10.1091/mbc.e12-01-0014 · DOI
  91. Kim, 2010, Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking, Biochem. Biophys. Res. Commun., 403, 167, 10.1016/j.bbrc.2010.10.121 · DOI
  92. Pan, 2017, Sortilin and retromer mediate retrograde transport of Glut4 in 3T3-L1 adipocytes, Mol. Biol. Cell, 28, 1667, 10.1091/mbc.e16-11-0777 · DOI · Paper page
  93. Seaman, 2004, Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer, J. Cell Biol., 165, 111, 10.1083/jcb.200312034 · DOI · Paper page
  94. Kovtun, 2018, Structure of the membrane-assembled retromer coat determined by cryo-electron tomography, Nature, 561, 561, 10.1038/s41586-018-0526-z · DOI · Paper page
  95. Nielsen, 2008, Different motifs regulate trafficking of SorCS1 isoforms, Traffic, 9, 980, 10.1111/j.1600-0854.2008.00731.x · DOI
  96. Lane, 2013, Protein sorting motifs in the cytoplasmic tail of SorCS1 control generation of Alzheimer's amyloid-beta peptide, J. Neurosci., 33, 7099, 10.1523/JNEUROSCI.5270-12.2013 · DOI
  97. Hermey, 2015, SorCS1 variants and amyloid precursor protein (APP) are co-transported in neurons but only SorCS1c modulates anterograde APP transport, J. Neurochem., 135, 60, 10.1111/jnc.13221 · DOI
  98. Rogaeva, 2007, The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease, Nat. Genet., 39, 168, 10.1038/ng1943 · DOI · Paper page
  99. Offe, 2006, The lipoprotein receptor LR11 regulates amyloid beta production and amyloid precursor protein traffic in endosomal compartments, J. Neurosci., 26, 1596, 10.1523/JNEUROSCI.4946-05.2006 · DOI · Paper page
  100. Madsen, 2019, HSPA12A targets the cytoplasmic domain and affects the trafficking of the amyloid precursor protein receptor SorLA, Sci. Rep., 9, 10.1038/s41598-018-37336-6 · DOI · Paper page

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Metadata

Authors
Malik, A. R., & Willnow, T. E.
Venue
Trends in Neurosciences
Publisher
Elsevier BV
Published
2020-11
Volume
43
Issue
11
Pages
870-885
ISSN
0166-2236
DOI
10.1016/j.tins.2020.08.003
Cited by
56
References
8
Language
en
Licence
Funders
  • Novo Nordisk Fonden
  • Fundacja na rzecz Nauki Polskiej
  • European Commission

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