메뉴 건너뛰기




Volumn 210, Issue 6, 2015, Pages 991-1002

Prosaposin facilitates sortilin-independent lysosomal trafficking of progranulin

Author keywords

[No Author keywords available]

Indexed keywords

LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; PROSAPOSIN; SOMATOMEDIN B RECEPTOR; SORTILIN; CATION-DEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR; GRN PROTEIN, HUMAN; GRN PROTEIN, MOUSE; LOW DENSITY LIPOPROTEIN RECEPTOR; LRP1 PROTEIN, MOUSE; PROTEIN BINDING; PSAP PROTEIN, HUMAN; PSAP PROTEIN, MOUSE; SIGNAL PEPTIDE; SPHINGOLIPID ACTIVATOR PROTEIN; TUMOR SUPPRESSOR PROTEIN; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84960380361     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201502029     Document Type: Article
Times cited : (144)

References (51)
  • 1
    • 33847654643 scopus 로고    scopus 로고
    • Progranulin in frontotemporal lobar degeneration and neuroinflammation
    • Ahmed, Z., I.R. Mackenzie, M.L. Hutton, and D.W. Dickson. 2007. Progranulin in frontotemporal lobar degeneration and neuroinflammation. J. Neuroinflammation. 4:7. http://dx.doi.org/10.1186/1742-2094-4-7
    • (2007) J. Neuroinflammation. , vol.4 , pp. 7
    • Ahmed, Z.1    Mackenzie, I.R.2    Hutton, M.L.3    Dickson, D.W.4
  • 2
    • 77954578417 scopus 로고    scopus 로고
    • Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging
    • Ahmed, Z., H. Sheng, Y.F. Xu, W.L. Lin, A.E. Innes, J. Gass, X. Yu, C.A. Wuertzer, H. Hou, S. Chiba, et al. 2010. Accelerated lipofuscinosis and ubiquitination in granulin knockout mice suggest a role for progranulin in successful aging. Am. J. Pathol. 177:311-324. http://dx.doi.org/10.2353/ajpath.2010.090915
    • (2010) Am. J. Pathol. , vol.177 , pp. 311-324
    • Ahmed, Z.1    Sheng, H.2    Xu, Y.F.3    Lin, W.L.4    Innes, A.E.5    Gass, J.6    Yu, X.7    Wuertzer, C.A.8    Hou, H.9    Chiba, S.10
  • 3
    • 80054737024 scopus 로고    scopus 로고
    • Progranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteins
    • Almeida, S., L. Zhou, and F.B. Gao. 2011. Progranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteins. PLoS ONE. 6:e26454. http://dx.doi. org/10.1371/journal.pone.0026454
    • (2011) PLoS ONE. , vol.6
    • Almeida, S.1    Zhou, L.2    Gao, F.B.3
  • 5
    • 84866135706 scopus 로고    scopus 로고
    • Culturing pyramidal neurons from the early postnatal mouse hippocampus and cortex
    • Beaudoin, G.M. III, S.H. Lee, D. Singh, Y. Yuan, Y.G. Ng, L.F. Reichardt, and J. Arikkath. 2012. Culturing pyramidal neurons from the early postnatal mouse hippocampus and cortex. Nat. Protoc. 7:1741-1754. http://dx.doi. org/10.1038/nprot.2012.099
    • (2012) Nat. Protoc. , vol.7 , pp. 1741-1754
    • Beaudoin, G.M.1    Lee, S.H.2    Singh, D.3    Yuan, Y.4    Ng, Y.G.5    Reichardt, L.F.6    Arikkath, J.7
  • 7
    • 77956063541 scopus 로고    scopus 로고
    • Pathophysiology of neuropathic lysosomal storage disorders
    • Bellettato, C.M., and M. Scarpa. 2010. Pathophysiology of neuropathic lysosomal storage disorders. J. Inherit. Metab. Dis. 33:347-362. http://dx.doi. org/10.1007/s10545-010-9075-9
    • (2010) J. Inherit. Metab. Dis. , vol.33 , pp. 347-362
    • Bellettato, C.M.1    Scarpa, M.2
  • 8
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and F.P. Cordelières. 2006. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224:213-232. http://dx.doi. org/10.1111/j.1365-2818.2006.01706.x
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 9
    • 84873050230 scopus 로고    scopus 로고
    • The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function
    • Brady, O.A., Y. Zheng, K. Murphy, M. Huang, and F. Hu. 2013. The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function. Hum. Mol. Genet. 22:685-695. http://dx.doi. org/10.1093/hmg/dds475
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 685-695
    • Brady, O.A.1    Zheng, Y.2    Murphy, K.3    Huang, M.4    Hu, F.5
  • 10
    • 84866536050 scopus 로고    scopus 로고
    • Progranulin: a proteolytically processed protein at the crossroads of inflammation and neurodegeneration
    • Cenik, B., C.F. Sephton, B. Kutluk Cenik, J. Herz, and G. Yu. 2012. Progranulin: a proteolytically processed protein at the crossroads of inflammation and neurodegeneration. J. Biol. Chem. 287:32298-32306. http://dx.doi. org/10.1074/jbc.R112.399170
    • (2012) J. Biol. Chem. , vol.287 , pp. 32298-32306
    • Cenik, B.1    Sephton, C.F.2    Kutluk Cenik, B.3    Herz, J.4    Yu, G.5
  • 13
    • 84869014351 scopus 로고    scopus 로고
    • Disruption of protein quality control in Parkinson's disease
    • Cook, C., C. Stetler, and L. Petrucelli. 2012. Disruption of protein quality control in Parkinson's disease. Cold Spring Harb. Perspect. Med. 2:a009423. http://dx.doi.org/10.1101/cshperspect.a009423
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2
    • Cook, C.1    Stetler, C.2    Petrucelli, L.3
  • 16
    • 64849103956 scopus 로고    scopus 로고
    • Plasma progranulin levels predict progranulin mutation status in frontotemporal dementia patients and asymptomatic family members
    • Finch, N., M. Baker, R. Crook, K. Swanson, K. Kuntz, R. Surtees, G. Bisceglio, A. Rovelet-Lecrux, B. Boeve, R.C. Petersen, et al. 2009. Plasma progranulin levels predict progranulin mutation status in frontotemporal dementia patients and asymptomatic family members. Brain. 132:583-591. http://dx.doi.org/10.1093/brain/awn352
    • (2009) Brain. , vol.132 , pp. 583-591
    • Finch, N.1    Baker, M.2    Crook, R.3    Swanson, K.4    Kuntz, K.5    Surtees, R.6    Bisceglio, G.7    Rovelet-Lecrux, A.8    Boeve, B.9    Petersen, R.C.10
  • 17
    • 0029982572 scopus 로고    scopus 로고
    • Targeted disruption of the mouse sphingolipid activator protein gene: a complex phenotype, including severe leukodystrophy and wide-spread storage of multiple sphingolipids
    • Fujita, N., K. Suzuki, M.T. Vanier, B. Popko, N. Maeda, A. Klein, M. Henseler, K. Sandhoff, H. Nakayasu, and K. Suzuki. 1996. Targeted disruption of the mouse sphingolipid activator protein gene: a complex phenotype, including severe leukodystrophy and wide-spread storage of multiple sphingolipids. Hum. Mol. Genet. 5:711-725. http://dx.doi.org/10.1093/ hmg/5.6.711
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 711-725
    • Fujita, N.1    Suzuki, K.2    Vanier, M.T.3    Popko, B.4    Maeda, N.5    Klein, A.6    Henseler, M.7    Sandhoff, K.8    Nakayasu, H.9    Suzuki, K.10
  • 19
    • 54449085260 scopus 로고    scopus 로고
    • Low plasma progranulin levels predict progranulin mutations in frontotemporal lobar degeneration
    • Ghidoni, R., L. Benussi, M. Glionna, M. Franzoni, and G. Binetti. 2008. Low plasma progranulin levels predict progranulin mutations in frontotemporal lobar degeneration. Neurology. 71:1235-1239. http://dx.doi. org/10.1212/01.wnl.0000325058.10218.fc
    • (2008) Neurology. , vol.71 , pp. 1235-1239
    • Ghidoni, R.1    Benussi, L.2    Glionna, M.3    Franzoni, M.4    Binetti, G.5
  • 22
    • 0032541422 scopus 로고    scopus 로고
    • Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP)
    • Hiesberger, T., S. Hüttler, A. Rohlmann, W. Schneider, K. Sandhoff, and J. Herz. 1998. Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP). EMBO J. 17:4617-4625. http://dx.doi.org/10.1093/emboj/17.16.4617
    • (1998) EMBO J. , vol.17 , pp. 4617-4625
    • Hiesberger, T.1    Hüttler, S.2    Rohlmann, A.3    Schneider, W.4    Sandhoff, K.5    Herz, J.6
  • 24
    • 74049124412 scopus 로고    scopus 로고
    • Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
    • Ju, J.S., R.A. Fuentealba, S.E. Miller, E. Jackson, D. Piwnica-Worms, R.H. Baloh, and C.C. Weihl. 2009. Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease. J. Cell Biol. 187:875-888. http://dx.doi.org/10.1083/jcb.200908115
    • (2009) J. Cell Biol. , vol.187 , pp. 875-888
    • Ju, J.S.1    Fuentealba, R.A.2    Miller, S.E.3    Jackson, E.4    Piwnica-Worms, D.5    Baloh, R.H.6    Weihl, C.C.7
  • 26
    • 84861722031 scopus 로고    scopus 로고
    • Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration
    • Lang, C.M., K. Fellerer, B.M. Schwenk, P.H. Kuhn, E. Kremmer, D. Edbauer, A. Capell, and C. Haass. 2012. Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration. J. Biol. Chem. 287:19355- 19365. http://dx.doi.org/10.1074/jbc.M112.365098
    • (2012) J. Biol. Chem. , vol.287 , pp. 19355- 19365
    • Lang, C.M.1    Fellerer, K.2    Schwenk, B.M.3    Kuhn, P.H.4    Kremmer, E.5    Edbauer, D.6    Capell, A.7    Haass, C.8
  • 27
    • 58149340240 scopus 로고    scopus 로고
    • ESCRT, autophagy, and frontotemporal dementia
    • Lee, J.A., and F.B. Gao. 2008. ESCRT, autophagy, and frontotemporal dementia. BMB Rep. 41:827-832. http://dx.doi.org/10.5483/BMBRep.2008.41.12.827
    • (2008) BMB Rep. , vol.41 , pp. 827-832
    • Lee, J.A.1    Gao, F.B.2
  • 28
    • 0345732689 scopus 로고    scopus 로고
    • The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois, S., J. Zeng, A.J. Hassan, M. Canuel, and C.R. Morales. 2003. The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. EMBO J. 22:6430-6437. http://dx.doi.org/10.1093/emboj/ cdg629
    • (2003) EMBO J. , vol.22 , pp. 6430-6437
    • Lefrancois, S.1    Zeng, J.2    Hassan, A.J.3    Canuel, M.4    Morales, C.R.5
  • 29
    • 0030016109 scopus 로고    scopus 로고
    • Proteolytic processing patterns of prosaposin in insect and mammalian cells
    • Leonova, T., X. Qi, A. Bencosme, E. Ponce, Y. Sun, and G.A. Grabowski. 1996. Proteolytic processing patterns of prosaposin in insect and mammalian cells. J. Biol. Chem. 271:17312-17320. http://dx.doi.org/10.1074/ jbc.271.29.17312
    • (1996) J. Biol. Chem. , vol.271 , pp. 17312-17320
    • Leonova, T.1    Qi, X.2    Bencosme, A.3    Ponce, E.4    Sun, Y.5    Grabowski, G.A.6
  • 32
    • 38449095568 scopus 로고    scopus 로고
    • The function of sphingolipids in the nervous system: lessons learnt from mouse models of specific sphingolipid activator protein deficiencies
    • Matsuda, J., A. Yoneshige, and K. Suzuki. 2007. The function of sphingolipids in the nervous system: lessons learnt from mouse models of specific sphingolipid activator protein deficiencies. J. Neurochem. 103:32-38. http:// dx.doi.org/10.1111/j.1471-4159.2007.04709.x
    • (2007) J. Neurochem. , vol.103 , pp. 32-38
    • Matsuda, J.1    Yoneshige, A.2    Suzuki, K.3
  • 33
    • 84907883637 scopus 로고    scopus 로고
    • The protective role of prosaposin and its receptors in the nervous system
    • Meyer, R.C., M.M. Giddens, B.M. Coleman, and R.A. Hall. 2014. The protective role of prosaposin and its receptors in the nervous system. Brain Res. 1585:1-12. http://dx.doi.org/10.1016/j.brainres.2014.08.022
    • (2014) Brain Res. , vol.1585 , pp. 1-12
    • Meyer, R.C.1    Giddens, M.M.2    Coleman, B.M.3    Hall, R.A.4
  • 34
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease
    • Nixon, R.A., and A.M. Cataldo. 2006. Lysosomal system pathways: genes to neurodegeneration in Alzheimer's disease. J. Alzheimers Dis. 9:277-289.
    • (2006) J. Alzheimers Dis. , vol.9 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 35
    • 48249103491 scopus 로고    scopus 로고
    • Neurodegenerative lysosomal disorders: a continuum from development to late age
    • Nixon, R.A., D.S. Yang, and J.H. Lee. 2008. Neurodegenerative lysosomal disorders: a continuum from development to late age. Autophagy. 4:590-599. http://dx.doi.org/10.4161/auto.6259
    • (2008) Autophagy. , vol.4 , pp. 590-599
    • Nixon, R.A.1    Yang, D.S.2    Lee, J.H.3
  • 37
    • 0025897376 scopus 로고
    • Saposin proteins: structure, function, and role in human lysosomal storage disorders
    • O'Brien, J.S., and Y. Kishimoto. 1991. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 5:301-308.
    • (1991) FASEB J. , vol.5 , pp. 301-308
    • O'Brien, J.S.1    Kishimoto, Y.2
  • 38
    • 0025729050 scopus 로고
    • Biosynthesis of lysosomal enzymes in cells of the End3 complementation group conditionally defective in endosomal acidification
    • Park, J.E., R.K. Draper, and W.J. Brown. 1991. Biosynthesis of lysosomal enzymes in cells of the End3 complementation group conditionally defective in endosomal acidification. Somat. Cell Mol. Genet. 17:137-150. http://dx.doi.org/10.1007/BF01232971
    • (1991) Somat. Cell Mol. Genet. , vol.17 , pp. 137-150
    • Park, J.E.1    Draper, R.K.2    Brown, W.J.3
  • 39
    • 0035193420 scopus 로고    scopus 로고
    • Molecular and cell biology of acid ß-glucosidase and prosaposin
    • Qi, X., and G.A. Grabowski. 2001. Molecular and cell biology of acid ß-glucosidase and prosaposin. Prog. Nucleic Acid Res. Mol. Biol. 66:203-239. http://dx.doi.org/10.1016/S0079-6603(00)66030-0
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 203-239
    • Qi, X.1    Grabowski, G.A.2
  • 40
    • 39049122146 scopus 로고    scopus 로고
    • Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors
    • Qian, M., D.E. Sleat, H. Zheng, D. Moore, and P. Lobel. 2008. Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors. Mol. Cell. Proteomics. 7:58-70. http://dx.doi.org/10.1074/mcp.M700217-MCP200
    • (2008) Mol. Cell. Proteomics. , vol.7 , pp. 58-70
    • Qian, M.1    Sleat, D.E.2    Zheng, H.3    Moore, D.4    Lobel, P.5
  • 41
    • 44349133382 scopus 로고    scopus 로고
    • ESCRT functions in autophagy and associated disease
    • Rusten, T.E., and A. Simonsen. 2008. ESCRT functions in autophagy and associated disease. Cell Cycle. 7:1166-1172. http://dx.doi.org/10.4161/ cc.7.9.5784
    • (2008) Cell Cycle. , vol.7 , pp. 1166-1172
    • Rusten, T.E.1    Simonsen, A.2
  • 44
    • 25444512703 scopus 로고    scopus 로고
    • Gaucher disease mouse models: point mutations at the acid ß-glucosidase locus combined with low-level prosaposin expression lead to disease variants
    • Sun, Y., B. Quinn, D.P. Witte, and G.A. Grabowski. 2005. Gaucher disease mouse models: point mutations at the acid ß-glucosidase locus combined with low-level prosaposin expression lead to disease variants. J. Lipid Res. 46:2102-2113. http://dx.doi.org/10.1194/jlr.M500202-JLR200
    • (2005) J. Lipid Res. , vol.46 , pp. 2102-2113
    • Sun, Y.1    Quinn, B.2    Witte, D.P.3    Grabowski, G.A.4
  • 45
    • 84881220459 scopus 로고    scopus 로고
    • Increased lysosomal biogenesis in activated microglia and exacerbated neuronal damage after traumatic brain injury in progranulin-deficient mice
    • Tanaka, Y., T. Matsuwaki, K. Yamanouchi, and M. Nishihara. 2013. Increased lysosomal biogenesis in activated microglia and exacerbated neuronal damage after traumatic brain injury in progranulin-deficient mice. Neuroscience. 250:8-19. http://dx.doi.org/10.1016/j.neuroscience.2013.06.049
    • (2013) Neuroscience. , vol.250 , pp. 8-19
    • Tanaka, Y.1    Matsuwaki, T.2    Yamanouchi, K.3    Nishihara, M.4
  • 46
    • 13244291416 scopus 로고    scopus 로고
    • Use of polyethyleneimine polymer in cell culture as attachment factor and lipofection enhancer
    • Vancha, A.R., S. Govindaraju, K.V. Parsa, M. Jasti, M. González-García, and R.P. Ballestero. 2004. Use of polyethyleneimine polymer in cell culture as attachment factor and lipofection enhancer. BMC Biotechnol. 4:23. http://dx.doi.org/10.1186/1472-6750-4-23
    • (2004) BMC Biotechnol. , vol.4 , pp. 23
    • Vancha, A.R.1    Govindaraju, S.2    Parsa, K.V.3    Jasti, M.4    González-García, M.5    Ballestero, R.P.6
  • 47
  • 48
    • 76149118401 scopus 로고    scopus 로고
    • Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice
    • Yin, F., R. Banerjee, B. Thomas, P. Zhou, L. Qian, T. Jia, X. Ma, Y. Ma, C. Iadecola, M.F. Beal, et al. 2010. Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice. J. Exp. Med. 207:117-128. http://dx.doi.org/10.1084/jem.20091568
    • (2010) J. Exp. Med. , vol.207 , pp. 117-128
    • Yin, F.1    Banerjee, R.2    Thomas, B.3    Zhou, P.4    Qian, L.5    Jia, T.6    Ma, X.7    Ma, Y.8    Iadecola, C.9    Beal, M.F.10
  • 49
    • 79958831842 scopus 로고    scopus 로고
    • C-terminus of progranulin interacts with the ß-propeller region of sortilin to regulate progranulin trafficking
    • Zheng, Y., O.A. Brady, P.S. Meng, Y. Mao, and F. Hu. 2011. C-terminus of progranulin interacts with the ß-propeller region of sortilin to regulate progranulin trafficking. PLoS ONE. 6:e21023. http://dx.doi.org/10.1371/journal.pone.0021023
    • (2011) PLoS ONE. , vol.6
    • Zheng, Y.1    Brady, O.A.2    Meng, P.S.3    Mao, Y.4    Hu, F.5
  • 50
    • 0028049917 scopus 로고
    • Intermolecular association of lysosomal protein precursors during biosynthesis
    • Zhu, Y., and G.E. Conner. 1994. Intermolecular association of lysosomal protein precursors during biosynthesis. J. Biol. Chem. 269:3846-3851.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3846-3851
    • Zhu, Y.1    Conner, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.