메뉴 건너뛰기




Volumn 16, Issue 3, 2015, Pages 126-132

Retromer in Alzheimer disease, Parkinson disease and other neurological disorders

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; ADAPTOR PROTEIN;

EID: 84923647965     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn3896     Document Type: Article
Times cited : (186)

References (93)
  • 1
    • 79952540486 scopus 로고    scopus 로고
    • Charting the secretory pathway in a simple eukaryote
    • Schekman, R. Charting the secretory pathway in a simple eukaryote. Mol. Biol. Cell 21, 3781-3784 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3781-3784
    • Schekman, R.1
  • 3
    • 0031823307 scopus 로고    scopus 로고
    • A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast
    • Seaman, M. N., McCaffery, J. M. & Emr, S. D. A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J. Cell Biol. 142, 665-681 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 665-681
    • Seaman, M.N.1    McCaffery, J.M.2    Emr, S.D.3
  • 4
    • 0033634771 scopus 로고    scopus 로고
    • Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: Assembly into multimeric complexes
    • Haft, C. R. et al. Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. Mol. Biol. Cell 11, 4105-4116 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4105-4116
    • Haft, C.R.1
  • 5
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M. N. Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 6
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R. & Bonifacino, J. S. Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123-133 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 123-133
    • Arighi, C.N.1    Hartnell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 7
    • 27744576858 scopus 로고    scopus 로고
    • Model-guided microarray implicates the retromer complex in Alzheimer's disease
    • Small, S. A. et al. Model-guided microarray implicates the retromer complex in Alzheimer's disease. Ann. Neurol. 58, 909-919 (2005).
    • (2005) Ann. Neurol. , vol.58 , pp. 909-919
    • Small, S.A.1
  • 8
    • 84891658400 scopus 로고    scopus 로고
    • Retromer: A master conductor of endosome sorting
    • Burd, C. & Cullen, P. J. Retromer: a master conductor of endosome sorting. Cold Spring Harb. Perspect. Biol. 6, a016774 (2014).
    • (2014) Cold Spring Harb. Perspect. Biol. , vol.6 , pp. a016774
    • Burd, C.1    Cullen, P.J.2
  • 10
    • 84897411251 scopus 로고    scopus 로고
    • Retromer mediates a discrete route of local membrane delivery to dendrites
    • Choy, R. W. et al. Retromer mediates a discrete route of local membrane delivery to dendrites. Neuron 82, 55-62 (2014).
    • (2014) Neuron , vol.82 , pp. 55-62
    • Choy, R.W.1
  • 11
    • 84863012293 scopus 로고    scopus 로고
    • RAB-6.2 and the retromer regulate glutamate receptor recycling through a retrograde pathway
    • Zhang, D. et al. RAB-6.2 and the retromer regulate glutamate receptor recycling through a retrograde pathway. J. Cell Biol. 196, 85-101 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 85-101
    • Zhang, D.1
  • 12
  • 14
    • 79955073671 scopus 로고    scopus 로고
    • Retromer terminates the generation of cAMP by internalized PTH receptors
    • Feinstein, T. N. et al. Retromer terminates the generation of cAMP by internalized PTH receptors. Nature Chem. Biol. 7, 278-284 (2011).
    • (2011) Nature Chem. Biol. , vol.7 , pp. 278-284
    • Feinstein, T.N.1
  • 15
    • 79957914861 scopus 로고    scopus 로고
    • SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors
    • Temkin, P. et al. SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors. Nature Cell Biol. 13, 715-721 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 715-721
    • Temkin, P.1
  • 16
    • 13244275069 scopus 로고    scopus 로고
    • Recycle your receptors with retromer
    • Seaman, M. N. Recycle your receptors with retromer. Trends Cell Biol. 15, 68-75 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 68-75
    • Seaman, M.N.1
  • 17
    • 26944480746 scopus 로고    scopus 로고
    • A novel mammalian retromer component, Vps26B
    • Kerr, M. C. et al. A novel mammalian retromer component, Vps26B. Traffic 6, 991-1001 (2005).
    • (2005) Traffic , vol.6 , pp. 991-1001
    • Kerr, M.C.1
  • 18
    • 38849094724 scopus 로고    scopus 로고
    • Structure of Vps26B and mapping of its interaction with the retromer protein complex
    • Collins, B. M. et al. Structure of Vps26B and mapping of its interaction with the retromer protein complex. Traffic 9, 366-379 (2008).
    • (2008) Traffic , vol.9 , pp. 366-379
    • Collins, B.M.1
  • 19
    • 50349086394 scopus 로고    scopus 로고
    • Identification of novel retromer complexes in the mouse testis
    • Kim, E. et al. Identification of novel retromer complexes in the mouse testis. Biochem. Biophys. Res. Commun. 375, 16-21 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.375 , pp. 16-21
    • Kim, E.1
  • 20
    • 81055140198 scopus 로고    scopus 로고
    • Vps26A and Vps26B subunits define distinct retromer complexes
    • Bugarcic, A. et al. Vps26A and Vps26B subunits define distinct retromer complexes. Traffic 12, 1759-1773 (2011).
    • (2011) Traffic , vol.12 , pp. 1759-1773
    • Bugarcic, A.1
  • 21
    • 84907228011 scopus 로고    scopus 로고
    • A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer
    • Gallon, M. et al. A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer. Proc. Natl Acad. Sci. USA 111, E3604-E3613 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E3604-E3613
    • Gallon, M.1
  • 22
    • 78649906977 scopus 로고    scopus 로고
    • Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking
    • Kim, E. et al. Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking. Biochem. Biophys. Res. Commun. 403, 167-171 (2010).
    • (2010) Biochem. Biophys. Res. Commun. , vol.403 , pp. 167-171
    • Kim, E.1
  • 24
    • 33846587097 scopus 로고    scopus 로고
    • Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors
    • Rojas, R., Kametaka, S., Haft, C. R. & Bonifacino, J. S. Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. Mol. Cell. Biol. 27, 1112-1124 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1112-1124
    • Rojas, R.1    Kametaka, S.2    Haft, C.R.3    Bonifacino, J.S.4
  • 25
    • 33846811334 scopus 로고    scopus 로고
    • A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer
    • Wassmer, T. et al. A loss-of-function screen reveals SNX5 and SNX6 as potential components of the mammalian retromer. J. Cell Sci. 120, 45-54 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 45-54
    • Wassmer, T.1
  • 26
    • 84907201006 scopus 로고    scopus 로고
    • Rapid mapping of interactions between human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy
    • Sierecki, E. et al. Rapid mapping of interactions between human SNX-BAR proteins measured in vitro by AlphaScreen and single-molecule spectroscopy. Mol. Cell. Proteom. 13, 2233-2245 (2014).
    • (2014) Mol. Cell. Proteom. , vol.13 , pp. 2233-2245
    • Sierecki, E.1
  • 27
    • 84870541192 scopus 로고    scopus 로고
    • Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules
    • van Weering, J. R. et al. Molecular basis for SNX-BAR-mediated assembly of distinct endosomal sorting tubules. EMBO J. 31, 4466-4480 (2012).
    • (2012) EMBO J. , vol.31 , pp. 4466-4480
    • Van Weering, J.R.1
  • 28
    • 78149347707 scopus 로고    scopus 로고
    • The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics
    • Harbour, M. E. et al. The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics. J. Cell Sci. 123, 3703-3717 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 3703-3717
    • Harbour, M.E.1
  • 29
    • 79961002971 scopus 로고    scopus 로고
    • A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion
    • Harterink, M. et al. A SNX3-dependent retromer pathway mediates retrograde transport of the Wnt sorting receptor Wntless and is required for Wnt secretion. Nature Cell Biol. 13, 914-923 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 914-923
    • Harterink, M.1
  • 30
    • 56149112942 scopus 로고    scopus 로고
    • Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7
    • Rojas, R. et al. Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7. J. Cell Biol. 183, 513-526 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 513-526
    • Rojas, R.1
  • 31
    • 69649083104 scopus 로고    scopus 로고
    • Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5
    • Seaman, M. N., Harbour, M. E., Tattersall, D., Read, E. & Bright, N. Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5. J. Cell Sci. 122, 2371-2382 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 2371-2382
    • Seaman, M.N.1    Harbour, M.E.2    Tattersall, D.3    Read, E.4    Bright, N.5
  • 32
    • 84891919318 scopus 로고    scopus 로고
    • A mechanism for retromer endosomal coat complex assembly with cargo
    • Harrison, M. S. et al. A mechanism for retromer endosomal coat complex assembly with cargo. Proc. Natl Acad. Sci. USA 111, 267-272 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 267-272
    • Harrison, M.S.1
  • 33
    • 0037073673 scopus 로고    scopus 로고
    • The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation
    • Cozier, G. E. et al. The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation. J. Biol. Chem. 277, 48730-48736 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 48730-48736
    • Cozier, G.E.1
  • 34
    • 84877293857 scopus 로고    scopus 로고
    • A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport
    • Steinberg, F. et al. A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport. Nature Cell Biol. 15, 461-471 (2013).
    • (2013) Nature Cell Biol. , vol.15 , pp. 461-471
    • Steinberg, F.1
  • 35
    • 78049265050 scopus 로고    scopus 로고
    • Evolutionary conservation of the WASH complex, an actin polymerization machine involved in endosomal fission
    • Derivery, E. & Gautreau, A. Evolutionary conservation of the WASH complex, an actin polymerization machine involved in endosomal fission. Commun. Integr. Biol. 3, 227-230 (2010).
    • (2010) Commun. Integr. Biol. , vol.3 , pp. 227-230
    • Derivery, E.1    Gautreau, A.2
  • 36
    • 71549167371 scopus 로고    scopus 로고
    • A FAM21-containing WASH complex regulates retromer-dependent sorting
    • Gomez, T. S. & Billadeau, D. D. A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev. Cell 17, 699-711 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 699-711
    • Gomez, T.S.1    Billadeau, D.D.2
  • 37
    • 84884185631 scopus 로고    scopus 로고
    • Microglial beclin 1 regulates retromer trafficking and phagocytosis and is impaired in Alzheimer's disease
    • Lucin, K. M. et al. Microglial beclin 1 regulates retromer trafficking and phagocytosis and is impaired in Alzheimer's disease. Neuron 79, 873-886 (2013).
    • (2013) Neuron , vol.79 , pp. 873-886
    • Lucin, K.M.1
  • 38
    • 33846613222 scopus 로고    scopus 로고
    • The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
    • Rogaeva, E. et al. The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease. Nature Genet. 39, 168-177 (2007).
    • (2007) Nature Genet. , vol.39 , pp. 168-177
    • Rogaeva, E.1
  • 39
    • 44449165118 scopus 로고    scopus 로고
    • Retromer deficiency observed in Alzheimer's disease causes hippocampal dysfunction, neurodegeneration, and Aβ accumulation
    • Muhammad, A. et al. Retromer deficiency observed in Alzheimer's disease causes hippocampal dysfunction, neurodegeneration, and Aβ accumulation. Proc. Natl Acad. Sci. USA 105, 7327-7332 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7327-7332
    • Muhammad, A.1
  • 40
    • 84861230374 scopus 로고    scopus 로고
    • The location and trafficking routes of the neuronal retromer and its role in amyloid precursor protein transport
    • Bhalla, A. et al. The location and trafficking routes of the neuronal retromer and its role in amyloid precursor protein transport. Neurobiol. Dis. 47, 126-134 (2012).
    • (2012) Neurobiol. Dis. , vol.47 , pp. 126-134
    • Bhalla, A.1
  • 41
    • 84863011338 scopus 로고    scopus 로고
    • Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing
    • Fjorback, A. W. et al. Retromer binds the FANSHY sorting motif in SorLA to regulate amyloid precursor protein sorting and processing. J. Neurosci. 32, 1467-1480 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 1467-1480
    • Fjorback, A.W.1
  • 42
    • 84867270258 scopus 로고    scopus 로고
    • Vps10 family proteins and the retromer complex in aging-related neurodegeneration and diabetes
    • Lane, R. F. et al. Vps10 family proteins and the retromer complex in aging-related neurodegeneration and diabetes. J. Neurosci. 32, 14080-14086 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 14080-14086
    • Lane, R.F.1
  • 43
    • 33749042749 scopus 로고    scopus 로고
    • Sorting through the cell biology of Alzheimer's disease: Intracellular pathways to pathogenesis
    • Small, S. A. & Gandy, S. Sorting through the cell biology of Alzheimer's disease: intracellular pathways to pathogenesis. Neuron 52, 15-31 (2006).
    • (2006) Neuron , vol.52 , pp. 15-31
    • Small, S.A.1    Gandy, S.2
  • 45
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • Futerman, A. H. & van Meer, G. The cell biology of lysosomal storage disorders. Nature Rev. Mol. Cell Biol. 5, 554-565 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 46
    • 84900460616 scopus 로고    scopus 로고
    • Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy
    • Zavodszky, E. et al. Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy. Nature Commun. 5, 3828 (2014).
    • (2014) Nature Commun. , vol.5 , pp. 3828
    • Zavodszky, E.1
  • 47
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon, R. A. The role of autophagy in neurodegenerative disease. Nature Med. 19, 983-997 (2013).
    • (2013) Nature Med. , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 48
    • 84920740324 scopus 로고    scopus 로고
    • Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein
    • Dhungel, R. et al. Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron 85, 76-87 (2015).
    • (2015) Neuron , vol.85 , pp. 76-87
    • Dhungel, R.1
  • 49
    • 84874853965 scopus 로고    scopus 로고
    • Mechanisms of protein seeding in neurodegenerative diseases
    • Walker, L. C., Diamond, M. I., Duff, K. E. & Hyman, B. T. Mechanisms of protein seeding in neurodegenerative diseases. JAMA Neurol. 70, 304-310 (2013).
    • (2013) JAMA Neurol. , vol.70 , pp. 304-310
    • Walker, L.C.1    Diamond, M.I.2    Duff, K.E.3    Hyman, B.T.4
  • 50
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K. C. et al. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 338, 949-953 (2012).
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1
  • 51
    • 84908011629 scopus 로고    scopus 로고
    • Isolating pathogenic mechanisms embedded within the hippocampal circuit through regional vulnerability
    • Small, S. A. Isolating pathogenic mechanisms embedded within the hippocampal circuit through regional vulnerability. Neuron 84, 32-39 (2014).
    • (2014) Neuron , vol.84 , pp. 32-39
    • Small, S.A.1
  • 52
    • 35348904514 scopus 로고    scopus 로고
    • Imaging the Aβ-related neurotoxicity of Alzheimer disease
    • Moreno, H. et al. Imaging the Aβ-related neurotoxicity of Alzheimer disease. Arch. Neurol. 64, 1467-1477 (2007).
    • (2007) Arch. Neurol. , vol.64 , pp. 1467-1477
    • Moreno, H.1
  • 53
    • 33748536734 scopus 로고    scopus 로고
    • LR11/SorLA expression is reduced in sporadic Alzheimer disease but not in familial Alzheimer disease
    • Dodson, S. E. et al. LR11/SorLA expression is reduced in sporadic Alzheimer disease but not in familial Alzheimer disease. J. Neuropathol. Exp. Neurol. 65, 866-872 (2006).
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 866-872
    • Dodson, S.E.1
  • 54
    • 84888317489 scopus 로고    scopus 로고
    • Meta-analysis of 74, 046 individuals identifies 11 new susceptibility loci for Alzheimer's disease
    • Lambert, J. C. et al. Meta-analysis of 74, 046 individuals identifies 11 new susceptibility loci for Alzheimer's disease. Nature Genet. 45, 1452-1458 (2013).
    • (2013) Nature Genet. , vol.45 , pp. 1452-1458
    • Lambert, J.C.1
  • 55
    • 84863469061 scopus 로고    scopus 로고
    • Identification of Alzheimer disease-associated variants in genes that regulate retromer function
    • Vardarajan, B. N. et al. Identification of Alzheimer disease-associated variants in genes that regulate retromer function. Neurobiol. Aging 33, 2231.e15-2231.e30 (2012).
    • (2012) Neurobiol. Aging , vol.33 , pp. 2231e15-2231e30
    • Vardarajan, B.N.1
  • 56
    • 84878632939 scopus 로고    scopus 로고
    • Independent and epistatic effects of variants in VPS10-d receptors on Alzheimer disease risk and processing of the amyloid precursor protein (APP)
    • Reitz, C. et al. Independent and epistatic effects of variants in VPS10-d receptors on Alzheimer disease risk and processing of the amyloid precursor protein (APP). Transl Psychiatry 3, e256 (2013).
    • (2013) Transl Psychiatry , vol.3 , pp. e256
    • Reitz, C.1
  • 57
    • 84881324927 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-phosphate regulates sorting and processing of amyloid precursor protein through the endosomal system
    • Morel, E. et al. Phosphatidylinositol-3-phosphate regulates sorting and processing of amyloid precursor protein through the endosomal system. Nature Commun. 4, 2250 (2013).
    • (2013) Nature Commun. , vol.4 , pp. 2250
    • Morel, E.1
  • 58
    • 84862907635 scopus 로고    scopus 로고
    • VPS35 haploinsufficiency increases Alzheimer's disease neuropathology
    • Wen, L. et al. VPS35 haploinsufficiency increases Alzheimer's disease neuropathology. J. Cell Biol. 195, 765-779 (2011).
    • (2011) J. Cell Biol. , vol.195 , pp. 765-779
    • Wen, L.1
  • 59
    • 77957326612 scopus 로고    scopus 로고
    • Diabetes-associated SorCS1 regulates Alzheimer's amyloid-β metabolism: Evidence for involvement of SorL1 and the retromer complex
    • Lane, R. F. et al. Diabetes-associated SorCS1 regulates Alzheimer's amyloid-β metabolism: evidence for involvement of SorL1 and the retromer complex. J. Neurosci. 30, 13110-13115 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 13110-13115
    • Lane, R.F.1
  • 60
    • 77957684047 scopus 로고    scopus 로고
    • Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated
    • Vieira, S. I. et al. Retrieval of the Alzheimer's amyloid precursor protein from the endosome to the TGN is S655 phosphorylation state-dependent and retromer-mediated. Mol. Neurodegener. 5, 40 (2010).
    • (2010) Mol. Neurodegener. , vol.5 , pp. 40
    • Vieira, S.I.1
  • 61
    • 84901190201 scopus 로고    scopus 로고
    • Pharmacological chaperones stabilize retromer to limit APP processing
    • Mecozzi, V. J. et al. Pharmacological chaperones stabilize retromer to limit APP processing. Nature Chem. Biol. 10, 443-449 (2014).
    • (2014) Nature Chem. Biol. , vol.10 , pp. 443-449
    • Mecozzi, V.J.1
  • 62
    • 84864359816 scopus 로고    scopus 로고
    • Amyloid precursor protein (APP) traffics from the cell surface via endosomes for amyloid β (Aβ) production in the trans-Golgi network
    • Choy, R. W., Cheng, Z. & Schekman, R. Amyloid precursor protein (APP) traffics from the cell surface via endosomes for amyloid β (Aβ) production in the trans-Golgi network. Proc. Natl Acad. Sci. USA 109, E2077-E2082 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. E2077-E2082
    • Choy, R.W.1    Cheng, Z.2    Schekman, R.3
  • 63
    • 84872057940 scopus 로고    scopus 로고
    • TREM2 variants in Alzheimer's disease
    • Guerreiro, R. et al. TREM2 variants in Alzheimer's disease. N. Engl. J. Med. 368, 117-127 (2013).
    • (2013) N. Engl. J. Med. , vol.368 , pp. 117-127
    • Guerreiro, R.1
  • 64
    • 84904479732 scopus 로고    scopus 로고
    • TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis
    • Kleinberger, G. et al. TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis. Sci. Transl Med. 6, 243ra286 (2014).
    • (2014) Sci. Transl Med. , vol.6 , pp. 243ra286
    • Kleinberger, G.1
  • 65
    • 84897954445 scopus 로고    scopus 로고
    • Microglial dysfunction in brain aging and Alzheimer's disease
    • Mosher, K. I. & Wyss-Coray, T. Microglial dysfunction in brain aging and Alzheimer's disease. Biochem. Pharmacol. 88, 594-604 (2014).
    • (2014) Biochem. Pharmacol. , vol.88 , pp. 594-604
    • Mosher, K.I.1    Wyss-Coray, T.2
  • 66
    • 84872714502 scopus 로고    scopus 로고
    • Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons
    • Wu, J. W. et al. Small misfolded tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons. J. Biol. Chem. 288, 1856-1870 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 1856-1870
    • Wu, J.W.1
  • 67
    • 84891905725 scopus 로고    scopus 로고
    • Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology
    • Michel, C. H. et al. Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology. J. Biol. Chem. 289, 956-967 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 956-967
    • Michel, C.H.1
  • 68
    • 77957340035 scopus 로고    scopus 로고
    • Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo
    • Khurana, V. et al. Lysosomal dysfunction promotes cleavage and neurotoxicity of tau in vivo. PLoS Genet. 6, e1001026 (2010).
    • (2010) PLoS Genet. , vol.6 , pp. e1001026
    • Khurana, V.1
  • 69
    • 80051534540 scopus 로고    scopus 로고
    • A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease
    • Zimprich, A. et al. A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease. Am. J. Hum. Genet. 89, 168-175 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 168-175
    • Zimprich, A.1
  • 70
    • 80051488602 scopus 로고    scopus 로고
    • VPS35 mutations in Parkinson disease
    • Vilarino-Guell, C. et al. VPS35 mutations in Parkinson disease. Am. J. Hum. Genet. 89, 162-167 (2011).
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 162-167
    • Vilarino-Guell, C.1
  • 71
    • 84873281274 scopus 로고    scopus 로고
    • RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk
    • Macleod, D. A. et al. RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson's disease risk. Neuron 77, 425-439 (2013).
    • (2013) Neuron , vol.77 , pp. 425-439
    • MacLeod, D.A.1
  • 73
    • 84892489531 scopus 로고    scopus 로고
    • The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer
    • Follett, J. et al. The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer. Traffic 15, 230-244 (2014).
    • (2014) Traffic , vol.15 , pp. 230-244
    • Follett, J.1
  • 74
    • 84906573100 scopus 로고    scopus 로고
    • Vacuolar protein sorting 35 (Vps35) rescues locomotor deficits and shortened lifespan in Drosophila expressing a Parkinson's disease mutant of leucine-rich repeat kinase 2 (LRRK2)
    • Linhart, R. et al. Vacuolar protein sorting 35 (Vps35) rescues locomotor deficits and shortened lifespan in Drosophila expressing a Parkinson's disease mutant of leucine-rich repeat kinase 2 (LRRK2). Mol. Neurodegener. 9, 23 (2014).
    • (2014) Mol. Neurodegener. , vol.9 , pp. 23
    • Linhart, R.1
  • 75
    • 84905025389 scopus 로고    scopus 로고
    • Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation
    • McGough, I. J. et al. Retromer binding to FAM21 and the WASH complex is perturbed by the Parkinson disease-linked VPS35(D620N) mutation. Curr. Biol. 24, 1670-1676 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1670-1676
    • McGough, I.J.1
  • 76
    • 84906503242 scopus 로고    scopus 로고
    • VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease
    • Miura, E. et al. VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease. Neurobiol. Dis. 71, 1-13 (2014).
    • (2014) Neurobiol. Dis. , vol.71 , pp. 1-13
    • Miura, E.1
  • 77
    • 84905646690 scopus 로고    scopus 로고
    • Parkinson's disease-linked mutations in VPS35 induce dopaminergic neurodegeneration
    • Tsika, E. et al. Parkinson's disease-linked mutations in VPS35 induce dopaminergic neurodegeneration. Hum. Mol. Genet. 23, 4621-4638 (2014).
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 4621-4638
    • Tsika, E.1
  • 78
    • 84919674911 scopus 로고    scopus 로고
    • Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo
    • Dodson, M. W., Leung, L. K., Lone, M., Lizzio, M. A. & Guo, M. Novel ethyl methanesulfonate (EMS)-induced null alleles of the Drosophila homolog of LRRK2 reveal a crucial role in endolysosomal functions and autophagy in vivo. Dis. Model. Mech. 7, 1351-1363 (2014).
    • (2014) Dis. Model. Mech. , vol.7 , pp. 1351-1363
    • Dodson, M.W.1    Leung, L.K.2    Lone, M.3    Lizzio, M.A.4    Guo, M.5
  • 79
    • 84877254679 scopus 로고    scopus 로고
    • Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome
    • Wang, X. et al. Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome. Nature Med. 19, 473-480 (2013).
    • (2013) Nature Med. , vol.19 , pp. 473-480
    • Wang, X.1
  • 80
    • 78650415043 scopus 로고    scopus 로고
    • Hereditary spastic paraplegias: Membrane traffic and the motor pathway
    • Blackstone, C., O'Kane, C. J. & Reid, E. Hereditary spastic paraplegias: membrane traffic and the motor pathway. Nature Rev. Neurosci. 12, 31-42 (2011).
    • (2011) Nature Rev. Neurosci. , vol.12 , pp. 31-42
    • Blackstone, C.1    O'Kane, C.J.2    Reid, E.3
  • 81
    • 33845991876 scopus 로고    scopus 로고
    • Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic paraplegia
    • Valdmanis, P. N. et al. Mutations in the KIAA0196 gene at the SPG8 locus cause hereditary spastic paraplegia. Am. J. Hum. Genet. 80, 152-161 (2007).
    • (2007) Am. J. Hum. Genet. , vol.80 , pp. 152-161
    • Valdmanis, P.N.1
  • 82
  • 83
    • 53849117085 scopus 로고    scopus 로고
    • Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor
    • Metcalf, D. J., Calvi, A. A., Seaman, M., Mitchison, H. M. & Cutler, D. F. Loss of the Batten disease gene CLN3 prevents exit from the TGN of the mannose 6-phosphate receptor. Traffic 9, 1905-1914 (2008).
    • (2008) Traffic , vol.9 , pp. 1905-1914
    • Metcalf, D.J.1    Calvi, A.A.2    Seaman, M.3    Mitchison, H.M.4    Cutler, D.F.5
  • 84
    • 84861379836 scopus 로고    scopus 로고
    • The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting
    • Mamo, A., Jules, F., Dumaresq-Doiron, K., Costantino, S. & Lefrancois, S. The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting. Mol. Cell. Biol. 32, 1855-1866 (2012).
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1855-1866
    • Mamo, A.1    Jules, F.2    Dumaresq-Doiron, K.3    Costantino, S.4    Lefrancois, S.5
  • 85
    • 33846657408 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulates the role of retromer in transcytosis of the polymeric immunoglobulin receptor
    • Verges, M., Sebastian, I. & Mostov, K. E. Phosphoinositide 3-kinase regulates the role of retromer in transcytosis of the polymeric immunoglobulin receptor. Exp. Cell Res. 313, 707-718 (2007).
    • (2007) Exp. Cell Res. , vol.313 , pp. 707-718
    • Verges, M.1    Sebastian, I.2    Mostov, K.E.3
  • 86
    • 84899580915 scopus 로고    scopus 로고
    • Neurodegeneration. Potential Alzheimer's drug spurs protein recycling
    • Garber, K. Neurodegeneration. Potential Alzheimer's drug spurs protein recycling. Science 344, 351 (2014).
    • (2014) Science , vol.344 , pp. 351
    • Garber, K.1
  • 87
    • 0034760183 scopus 로고    scopus 로고
    • Endocytic disturbances distinguish among subtypes of Alzheimer's disease and related disorders
    • Cataldo, A. et al. Endocytic disturbances distinguish among subtypes of Alzheimer's disease and related disorders. Ann. Neurol. 50, 661-665 (2001).
    • (2001) Ann. Neurol. , vol.50 , pp. 661-665
    • Cataldo, A.1
  • 88
    • 84856956771 scopus 로고    scopus 로고
    • Probing sporadic and familial Alzheimer's disease using induced pluripotent stem cells
    • Israel, M. A. et al. Probing sporadic and familial Alzheimer's disease using induced pluripotent stem cells. Nature 482, 216-220 (2012).
    • (2012) Nature , vol.482 , pp. 216-220
    • Israel, M.A.1
  • 89
    • 29444460533 scopus 로고    scopus 로고
    • Apolipoprotein (apo) E4 enhances amyloid β peptide production in cultured neuronal cells: ApoE structure as a potential therapeutic target
    • Ye, S. et al. Apolipoprotein (apo) E4 enhances amyloid β peptide production in cultured neuronal cells: apoE structure as a potential therapeutic target. Proc. Natl Acad. Sci. USA 102, 18700-18705 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18700-18705
    • Ye, S.1
  • 90
    • 84904678185 scopus 로고    scopus 로고
    • Apolipoprotein e in Alzheimer's disease: An update
    • Yu, J. T., Tan, L. & Hardy, J. Apolipoprotein E in Alzheimer's disease: an update. Ann. Rev. Neurosci. 37, 79-100 (2014).
    • (2014) Ann. Rev. Neurosci. , vol.37 , pp. 79-100
    • Yu, J.T.1    Tan, L.2    Hardy, J.3
  • 91
    • 84939599004 scopus 로고    scopus 로고
    • Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson's disease
    • Nalls, M. A. et al. Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson's disease. Nature Genet. 46, 989-993 (2014).
    • (2014) Nature Genet. , vol.46 , pp. 989-993
    • Nalls, M.A.1
  • 92
    • 84893763207 scopus 로고    scopus 로고
    • Molecular drivers and cortical spread of lateral entorhinal cortex dysfunction in preclinical Alzheimer's disease
    • Khan, U. A. et al. Molecular drivers and cortical spread of lateral entorhinal cortex dysfunction in preclinical Alzheimer's disease. Nature Neurosci. 17, 304-311 (2014).
    • (2014) Nature Neurosci. , vol.17 , pp. 304-311
    • Khan, U.A.1
  • 93
    • 84906678530 scopus 로고    scopus 로고
    • Pharmacological chaperones in the age of proteomic pathology
    • Small, S. A. Pharmacological chaperones in the age of proteomic pathology. Proc. Natl Acad. Sci. USA 111, 12274-12275 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 12274-12275
    • Small, S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.