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Volumn 18, Issue 1, 2017, Pages

Subcellular trafficking of mammalian lysosomal proteins: An extended view

Author keywords

Alternative receptor; Lysosome; Mannose 6 phosphate; Sorting motif; Trafficking; Unconventional

Indexed keywords

HYDROLASE; LEUCINE; MANNOSE 6 PHOSPHATE; MEMBRANE PROTEIN; TYROSINE DERIVATIVE; SIGNAL PEPTIDE;

EID: 85008238942     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms18010047     Document Type: Review
Times cited : (67)

References (176)
  • 1
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • De Duve, C., Pressman, B.C., Gianetto, R., Wattiaux, R., Appelmans, F. Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem. J. 1955, 60, 604-617. [CrossRef] [PubMed]
    • (1955) Biochem. J , vol.60 , pp. 604-617
    • De Duve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 2
    • 84882398449 scopus 로고    scopus 로고
    • Christian de Duve: Explorer of the cell who discovered new organelles by using a centrifuge
    • Sabatini, D.D., Adesnik, M. Christian de Duve: Explorer of the cell who discovered new organelles by using a centrifuge. Proc. Natl. Acad. Sci. USA 2013, 110, 13234-13235. [CrossRef] [PubMed]
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 13234-13235
    • Sabatini, D.D.1    Adesnik, M.2
  • 4
    • 60649108749 scopus 로고    scopus 로고
    • The integral membrane of lysosomes: Its proteins and their roles in disease
    • Callahan, J.W., Bagshaw, R.D., Mahuran, D.J. The integral membrane of lysosomes: Its proteins and their roles in disease. J. Proteom. 2009, 72, 23-33. [CrossRef] [PubMed]
    • (2009) J. Proteom , vol.72 , pp. 23-33
    • Callahan, J.W.1    Bagshaw, R.D.2    Mahuran, D.J.3
  • 5
    • 79953318188 scopus 로고    scopus 로고
    • Classification of subcellular location by comparative proteomic analysis of native and density-shifted lysosomes
    • Proteom. MCP 2011, 10, M110.006403
    • Della Valle, M.C., Sleat, D.E., Zheng, H., Moore, D.F., Jadot, M., Lobel, P. Classification of subcellular location by comparative proteomic analysis of native and density-shifted lysosomes. Mol. Cell. Proteom. MCP 2011, 10, M110.006403. [CrossRef] [PubMed]
    • Mol. Cell
    • Della Valle, M.C.1    Sleat, D.E.2    Zheng, H.3    Moore, D.F.4    Jadot, M.5    Lobel, P.6
  • 6
    • 84880056427 scopus 로고    scopus 로고
    • Extending the mannose 6-phosphate glycoproteome by high resolution/accuracy mass spectrometry analysis of control and acid phosphatase 5-deficient mice
    • Sleat, D.E., Sun, P., Wiseman, J.A., Huang, L., El-Banna, M., Zheng, H., Moore, D.F., Lobel, P. Extending the mannose 6-phosphate glycoproteome by high resolution/accuracy mass spectrometry analysis of control and acid phosphatase 5-deficient mice. Mol. Cell. Proteom. MCP 2013, 12, 1806-1817. [CrossRef] [PubMed]
    • (2013) Mol. Cell. Proteom. MCP , vol.12 , pp. 1806-1817
    • Sleat, D.E.1    Sun, P.2    Wiseman, J.A.3    Huang, L.4    El-Banna, M.5    Zheng, H.6    Moore, D.F.7    Lobel, P.8
  • 8
    • 62949116803 scopus 로고    scopus 로고
    • Lysosomal disorders: From storage to cellular damage
    • Ballabio, A., Gieselmann, V. Lysosomal disorders: From storage to cellular damage. Biochim. Biophys. Acta 2009, 1793, 684-696. [CrossRef] [PubMed]
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 684-696
    • Ballabio, A.1    Gieselmann, V.2
  • 9
    • 84871960929 scopus 로고    scopus 로고
    • The cell biology of disease: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction
    • Platt, F.M., Boland, B., van der Spoel, A.C. The cell biology of disease: Lysosomal storage disorders: The cellular impact of lysosomal dysfunction. J. Cell Biol. 2012, 199, 723-734. [CrossRef] [PubMed]
    • (2012) J. Cell Biol , vol.199 , pp. 723-734
    • Platt, F.M.1    Boland, B.2    Van Der Spoel, A.C.3
  • 10
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh, P., Dahms, N.M., Kornfeld, S. Mannose 6-phosphate receptors: New twists in the tale. Nat. Rev. Mol. Cell Biol. 2003, 4, 202-212. [CrossRef] [PubMed]
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 11
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J.S., Traub, L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 2003, 72, 395-447. [CrossRef] [PubMed]
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 12
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • Robinson, M.S. Adaptable adaptors for coated vesicles. Trends Cell Biol. 2004, 14, 167-174. [CrossRef] [PubMed]
    • (2004) Trends Cell Biol , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 13
    • 63149193317 scopus 로고    scopus 로고
    • Sorting of lysosomal proteins
    • Braulke, T., Bonifacino, J.S. Sorting of lysosomal proteins. Biochim. Biophys. Acta 2009, 1793, 605-614. [CrossRef] [PubMed]
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 605-614
    • Braulke, T.1    Bonifacino, J.S.2
  • 14
    • 84955173009 scopus 로고    scopus 로고
    • Forty years of Clathrin-coated vesicles
    • Robinson, M.S. Forty years of Clathrin-coated vesicles. Traffic (Cph. Den.) 2015, 16, 1210-1238. [CrossRef] [PubMed]
    • (2015) Traffic (Cph. Den.) , vol.16 , pp. 1210-1238
    • Robinson, M.S.1
  • 16
    • 84872038046 scopus 로고    scopus 로고
    • Adaptor protein complexes AP-4 and AP-5: New players in endosomal trafficking and progressive spastic paraplegia
    • Hirst, J., Irving, C., Borner, G.H.H. Adaptor protein complexes AP-4 and AP-5: New players in endosomal trafficking and progressive spastic paraplegia. Traffic (Cph. Den.) 2013, 14, 153-164. [CrossRef] [PubMed]
    • (2013) Traffic (Cph. Den.) , vol.14 , pp. 153-164
    • Hirst, J.1    Irving, C.2    Borner, G.H.H.3
  • 17
    • 69249227502 scopus 로고    scopus 로고
    • Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function
    • Saftig, P., Klumperman, J. Lysosome biogenesis and lysosomal membrane proteins: Trafficking meets function. Nat. Rev. Mol. Cell Biol. 2009, 10, 623-635. [CrossRef] [PubMed]
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 623-635
    • Saftig, P.1    Klumperman, J.2
  • 18
    • 84941899726 scopus 로고    scopus 로고
    • Loss of AP-5 results in accumulation of aberrant endolysosomes: Defining a new type of lysosomal storage disease
    • Hirst, J., Edgar, J.R., Esteves, T., Darios, F., Madeo, M., Chang, J., Roda, R.H., Dürr, A., Anheim, M., Gellera, C., et al. Loss of AP-5 results in accumulation of aberrant endolysosomes: Defining a new type of lysosomal storage disease. Hum. Mol. Genet. 2015, 24, 4984-4996. [CrossRef] [PubMed]
    • (2015) Hum. Mol. Genet , vol.24 , pp. 4984-4996
    • Hirst, J.1    Edgar, J.R.2    Esteves, T.3    Darios, F.4    Madeo, M.5    Chang, J.6    Roda, R.H.7    Dürr, A.8    Anheim, M.9    Gellera, C.10
  • 19
    • 0035918290 scopus 로고    scopus 로고
    • The targeting of cystinosin to the lysosomal membrane requires a tyrosine-based signal and a novel sorting motif
    • Cherqui, S., Kalatzis, V., Trugnan, G., Antignac, C. The targeting of cystinosin to the lysosomal membrane requires a tyrosine-based signal and a novel sorting motif. J. Biol. Chem. 2001, 276, 13314-13321. [CrossRef] [PubMed]
    • (2001) J. Biol. Chem , vol.276 , pp. 13314-13321
    • Cherqui, S.1    Kalatzis, V.2    Trugnan, G.3    Antignac, C.4
  • 21
    • 50549086057 scopus 로고    scopus 로고
    • Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb
    • Pryor, P.R., Jackson, L., Gray, S.R., Edeling, M.A., Thompson, A., Sanderson, C.M., Evans, P.R., Owen, D.J., Luzio, J.P. Molecular basis for the sorting of the SNARE VAMP7 into endocytic clathrin-coated vesicles by the ArfGAP Hrb. Cell 2008, 134, 817-827. [CrossRef] [PubMed]
    • (2008) Cell , vol.134 , pp. 817-827
    • Pryor, P.R.1    Jackson, L.2    Gray, S.R.3    Edeling, M.A.4    Thompson, A.5    Sanderson, C.M.6    Evans, P.R.7    Owen, D.J.8    Luzio, J.P.9
  • 24
    • 33751212452 scopus 로고    scopus 로고
    • Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination
    • Pak, Y., Glowacka, W.K., Bruce, M.C., Pham, N., Rotin, D. Transport of LAPTM5 to lysosomes requires association with the ubiquitin ligase Nedd4, but not LAPTM5 ubiquitination. J. Cell Biol. 2006, 175, 631-645. [CrossRef] [PubMed]
    • (2006) J. Cell Biol , vol.175 , pp. 631-645
    • Pak, Y.1    Glowacka, W.K.2    Bruce, M.C.3    Pham, N.4    Rotin, D.5
  • 25
    • 80855128821 scopus 로고    scopus 로고
    • A role for the ubiquitin ligase Nedd4 in membrane sorting of LAPTM4 proteins
    • Milkereit, R., Rotin, D. A role for the ubiquitin ligase Nedd4 in membrane sorting of LAPTM4 proteins. PLoS ONE 2011, 6, e27478. [CrossRef] [PubMed]
    • (2011) Plos ONE , pp. 6
    • Milkereit, R.1    Rotin, D.2
  • 26
    • 85015992433 scopus 로고    scopus 로고
    • Increased expression of the frontotemporal dementia risk factor TMEM106B causes C9orf72-dependent alterations in lysosomes
    • Busch, J.I., Unger, T.L., Jain, N., Tyler Skrinak, R., Charan, R.A., Chen-Plotkin, A.S. Increased expression of the frontotemporal dementia risk factor TMEM106B causes C9orf72-dependent alterations in lysosomes. Hum. Mol. Genet. 2016. [CrossRef] [PubMed]
    • (2016) Hum. Mol. Genet
    • Busch, J.I.1    Unger, T.L.2    Jain, N.3    Tyler Skrinak, R.4    Charan, R.A.5    Chen-Plotkin, A.S.6
  • 27
    • 11144231239 scopus 로고    scopus 로고
    • A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting
    • Storch, S., Pohl, S., Braulke, T. A dileucine motif and a cluster of acidic amino acids in the second cytoplasmic domain of the batten disease-related CLN3 protein are required for efficient lysosomal targeting. J. Biol. Chem. 2004, 279, 53625-53634. [CrossRef] [PubMed]
    • (2004) J. Biol. Chem , vol.279 , pp. 53625-53634
    • Storch, S.1    Pohl, S.2    Braulke, T.3
  • 28
    • 1542313968 scopus 로고    scopus 로고
    • Two motifs target Batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells
    • Kyttälä, A., Ihrke, G., Vesa, J., Schell, M.J., Luzio, J.P. Two motifs target Batten disease protein CLN3 to lysosomes in transfected nonneuronal and neuronal cells. Mol. Biol. Cell 2004, 15, 1313-1323. [CrossRef] [PubMed]
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1313-1323
    • Kyttälä, A.1    Ihrke, G.2    Vesa, J.3    Schell, M.J.4    Luzio, J.P.5
  • 29
    • 84982286015 scopus 로고    scopus 로고
    • What we know about TMEM106B in neurodegeneration
    • Nicholson, A.M., Rademakers, R. What we know about TMEM106B in neurodegeneration. Acta Neuropathol. 2016, 132, 639-651. [CrossRef] [PubMed]
    • (2016) Acta Neuropathol , vol.132 , pp. 639-651
    • Nicholson, A.M.1    Rademakers, R.2
  • 30
    • 84940796239 scopus 로고    scopus 로고
    • Cell biology of the NCL proteins: What they do and don’t do
    • Cárcel-Trullols, J., Kovács, A.D., Pearce, D.A. Cell biology of the NCL proteins: What they do and don’t do. Biochim. Biophys. Acta 2015, 1852, 2242-2255. [CrossRef] [PubMed]
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 2242-2255
    • Cárcel-Trullols, J.1    Kovács, A.D.2    Pearce, D.A.3
  • 31
    • 84990859087 scopus 로고    scopus 로고
    • Analysis of large-scale whole exome sequencing data to determine the prevalence of genetically-distinct forms of neuronal ceroid lipofuscinosis
    • Sleat, D.E., Gedvilaite, E., Zhang, Y., Lobel, P., Xing, J. Analysis of large-scale whole exome sequencing data to determine the prevalence of genetically-distinct forms of neuronal ceroid lipofuscinosis. Gene 2016, 593, 284-291. [CrossRef] [PubMed]
    • (2016) Gene , vol.593 , pp. 284-291
    • Sleat, D.E.1    Gedvilaite, E.2    Zhang, Y.3    Lobel, P.4    Xing, J.5
  • 32
    • 15444378335 scopus 로고    scopus 로고
    • AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif
    • Kyttälä, A., Yliannala, K., Schu, P., Jalanko, A., Luzio, J.P. AP-1 and AP-3 facilitate lysosomal targeting of Batten disease protein CLN3 via its dileucine motif. J. Biol. Chem. 2005, 280, 10277-10283. [CrossRef] [PubMed]
    • (2005) J. Biol. Chem , vol.280 , pp. 10277-10283
    • Kyttälä, A.1    Yliannala, K.2    Schu, P.3    Jalanko, A.4    Luzio, J.P.5
  • 33
    • 33745193071 scopus 로고    scopus 로고
    • An unconventional dileucine-based motif and a novel cytosolic motif are required for the lysosomal and melanosomal targeting of OA1
    • Piccirillo, R., Palmisano, I., Innamorati, G., Bagnato, P., Altimare, D., Schiaffino, M.V. An unconventional dileucine-based motif and a novel cytosolic motif are required for the lysosomal and melanosomal targeting of OA1. J. Cell Sci. 2006, 119, 2003-2014. [CrossRef] [PubMed]
    • (2006) J. Cell Sci , vol.119 , pp. 2003-2014
    • Piccirillo, R.1    Palmisano, I.2    Innamorati, G.3    Bagnato, P.4    Altimare, D.5    Schiaffino, M.V.6
  • 34
    • 84859715453 scopus 로고    scopus 로고
    • MLN64 transport to the late endosome is regulated by binding to 14-3-3 via a non-canonical binding site
    • Liapis, A., Chen, F.W., Davies, J.P., Wang, R., Ioannou, Y.A. MLN64 transport to the late endosome is regulated by binding to 14-3-3 via a non-canonical binding site. PLoS ONE 2012, 7, e34424. [CrossRef] [PubMed]
    • (2012) Plos ONE , vol.7
    • Liapis, A.1    Chen, F.W.2    Davies, J.P.3    Wang, R.4    Ioannou, Y.A.5
  • 35
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A.J., Xing, H. 14-3-3 proteins: Regulation of subcellular localization by molecular interference. Cell Signal. 2000, 12, 703-709. [CrossRef]
    • (2000) Cell Signal , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 36
    • 84864874958 scopus 로고    scopus 로고
    • MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
    • Martina, J.A., Chen, Y., Gucek, M., Puertollano, R. MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 2012, 8, 903-914. [CrossRef] [PubMed]
    • (2012) Autophagy , vol.8 , pp. 903-914
    • Martina, J.A.1    Chen, Y.2    Gucek, M.3    Puertollano, R.4
  • 37
    • 80054034515 scopus 로고    scopus 로고
    • Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport
    • Smith, A.J., Daut, J., Schwappach, B. Membrane proteins as 14-3-3 clients in functional regulation and intracellular transport. Physiology (Bethesda) 2011, 26, 181-191. [CrossRef] [PubMed]
    • (2011) Physiology (Bethesda) , vol.26 , pp. 181-191
    • Smith, A.J.1    Daut, J.2    Schwappach, B.3
  • 40
    • 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., Fellerer, K., Schwenk, B.M., Kuhn, P.-H., Kremmer, E., Edbauer, D., Capell, A., Haass, C. Membrane orientation and subcellular localization of transmembrane protein 106B (TMEM106B), a major risk factor for frontotemporal lobar degeneration. J. Biol. Chem. 2012, 287, 19355-19365. [CrossRef] [PubMed]
    • (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
  • 41
    • 84896134009 scopus 로고    scopus 로고
    • Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13 identify the PA domain as a determinant for endosomal localization
    • Van Dijk, J.R., Yamazaki, Y., Palmer, R.H. Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13 identify the PA domain as a determinant for endosomal localization. Biochem. J. 2014, 459, 27-36. [CrossRef] [PubMed]
    • (2014) Biochem. J , vol.459 , pp. 27-36
    • Van Dijk, J.R.1    Yamazaki, Y.2    Palmer, R.H.3
  • 42
    • 0035281597 scopus 로고    scopus 로고
    • The protease-associated domain: A homology domain associated with multiple classes of proteases
    • Luo, X., Hofmann, K. The protease-associated domain: A homology domain associated with multiple classes of proteases. Trends Biochem. Sci. 2001, 26, 147-148. [CrossRef]
    • (2001) Trends Biochem. Sci , vol.26 , pp. 147-148
    • Luo, X.1    Hofmann, K.2
  • 43
    • 84908243806 scopus 로고    scopus 로고
    • How vacuolar sorting receptor proteins interact with their cargo proteins: Crystal structures of apo and cargo-bound forms of the protease-associated domain from an Arabidopsis vacuolar sorting receptor
    • Luo, F., Fong, Y.H., Zeng, Y., Shen, J., Jiang, L., Wong, K.-B. How vacuolar sorting receptor proteins interact with their cargo proteins: Crystal structures of apo and cargo-bound forms of the protease-associated domain from an Arabidopsis vacuolar sorting receptor. Plant Cell 2014, 26, 3693-3708. [CrossRef] [PubMed]
    • (2014) Plant Cell , vol.26 , pp. 3693-3708
    • Luo, F.1    Fong, Y.H.2    Zeng, Y.3    Shen, J.4    Jiang, L.5    Wong, K.-B.6
  • 44
    • 33947245588 scopus 로고    scopus 로고
    • C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes
    • Storch, S., Pohl, S., Quitsch, A., Falley, K., Braulke, T. C-terminal prenylation of the CLN3 membrane glycoprotein is required for efficient endosomal sorting to lysosomes. Traffic (Cph. Den.) 2007, 8, 431-444. [CrossRef] [PubMed]
    • (2007) Traffic (Cph. Den.) , vol.8 , pp. 431-444
    • Storch, S.1    Pohl, S.2    Quitsch, A.3    Falley, K.4    Braulke, T.5
  • 45
    • 33644655372 scopus 로고    scopus 로고
    • Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes
    • Vergarajauregui, S., Puertollano, R. Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes. Traffic (Cph. Den.) 2006, 7, 337-353. [CrossRef] [PubMed]
    • (2006) Traffic (Cph. Den.) , vol.7 , pp. 337-353
    • Vergarajauregui, S.1    Puertollano, R.2
  • 46
    • 33744963797 scopus 로고    scopus 로고
    • Posttranslational cleavage and adaptor protein complex-dependent trafficking of mucolipin-1
    • Miedel, M.T., Weixel, K.M., Bruns, J.R., Traub, L.M., Weisz, O.A. Posttranslational cleavage and adaptor protein complex-dependent trafficking of mucolipin-1. J. Biol. Chem. 2006, 281, 12751-12759. [CrossRef] [PubMed]
    • (2006) J. Biol. Chem , vol.281 , pp. 12751-12759
    • Miedel, M.T.1    Weixel, K.M.2    Bruns, J.R.3    Traub, L.M.4    Weisz, O.A.5
  • 47
    • 78049511240 scopus 로고    scopus 로고
    • Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes
    • Flannery, A.R., Czibener, C., Andrews, N.W. Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes. J. Cell Biol. 2010, 191, 599-613. [CrossRef] [PubMed]
    • (2010) J. Cell Biol , vol.191 , pp. 599-613
    • Flannery, A.R.1    Czibener, C.2    Rews, N.W.3
  • 48
    • 84884411179 scopus 로고    scopus 로고
    • Anchors aweigh: Protein localization and transport mediated by transmembrane domains
    • Cosson, P., Perrin, J., Bonifacino, J.S. Anchors aweigh: Protein localization and transport mediated by transmembrane domains. Trends Cell Biol. 2013, 23, 511-517. [CrossRef] [PubMed]
    • (2013) Trends Cell Biol , vol.23 , pp. 511-517
    • Cosson, P.1    Perrin, J.2    Bonifacino, J.S.3
  • 49
    • 84935897756 scopus 로고    scopus 로고
    • Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein
    • Kiss, K., Kucsma, N., Brozik, A., Tusnady, G.E., Bergam, P., van Niel, G., Szakacs, G. Role of the N-terminal transmembrane domain in the endo-lysosomal targeting and function of the human ABCB6 protein. Biochem. J. 2015, 467, 127-139. [CrossRef] [PubMed]
    • (2015) Biochem. J. , vol.467 , pp. 127-139
    • Kiss, K.1    Kucsma, N.2    Brozik, A.3    Tusnady, G.E.4    Bergam, P.5    Van Niel, G.6    Szakacs, G.7
  • 50
    • 77949521198 scopus 로고    scopus 로고
    • Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain
    • Demirel, O., Bangert, I., Tampé, R., Abele, R. Tuning the cellular trafficking of the lysosomal peptide transporter TAPL by its N-terminal domain. Traffic (Cph. Den.) 2010, 11, 383-393. [CrossRef] [PubMed]
    • (2010) Traffic (Cph. Den.) , vol.11 , pp. 383-393
    • Demirel, O.1    Bangert, I.2    Tampé, R.3    Abele, R.4
  • 51
    • 84887500079 scopus 로고    scopus 로고
    • LMBD1 protein serves as a specific adaptor for insulin receptor internalization
    • Tseng, L.T.-L., Lin, C.-L., Tzen, K.-Y., Chang, S.C., Chang, M.-F. LMBD1 protein serves as a specific adaptor for insulin receptor internalization. J. Biol. Chem. 2013, 288, 32424-32432. [CrossRef] [PubMed]
    • (2013) J. Biol. Chem , vol.288 , pp. 32424-32432
    • Tseng, L.T.1    Lin, C.-L.2    Tzen, K.-Y.3    Chang, S.C.4    Chang, M.-F.5
  • 52
    • 84979516867 scopus 로고    scopus 로고
    • Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
    • Kawaguchi, K., Okamoto, T., Morita, M., Imanaka, T. Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1. Sci. Rep. 2016, 6, 30183. [CrossRef] [PubMed]
    • (2016) Sci. Rep , vol.6 , pp. 30183
    • Kawaguchi, K.1    Okamoto, T.2    Morita, M.3    Imanaka, T.4
  • 53
    • 84929997950 scopus 로고    scopus 로고
    • LAPTM4b recruits the LAT1-4F2hc Leu transporter to lysosomes and promotes mTORC1 activation
    • Milkereit, R., Persaud, A., Vanoaica, L., Guetg, A., Verrey, F., Rotin, D. LAPTM4b recruits the LAT1-4F2hc Leu transporter to lysosomes and promotes mTORC1 activation. Nat. Commun. 2015, 6, 7250. [CrossRef] [PubMed]
    • (2015) Nat. Commun , vol.6 , pp. 7250
    • Milkereit, R.1    Persaud, A.2    Vanoaica, L.3    Guetg, A.4    Verrey, F.5    Rotin, D.6
  • 54
    • 0025172954 scopus 로고
    • Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail
    • Williams, M.A., Fukuda, M. Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell Biol. 1990, 111, 955-966. [CrossRef] [PubMed]
    • (1990) J. Cell Biol , vol.111 , pp. 955-966
    • Williams, M.A.1    Fukuda, M.2
  • 55
    • 0029791503 scopus 로고    scopus 로고
    • The tyrosine-based lysosomal targeting signal in lamp-1 mediates sorting into Golgi-derived clathrin-coated vesicles
    • Höning, S., Griffith, J., Geuze, H.J., Hunziker, W. The tyrosine-based lysosomal targeting signal in lamp-1 mediates sorting into Golgi-derived clathrin-coated vesicles. EMBO J. 1996, 15, 5230-5239. [PubMed]
    • (1996) EMBO J , vol.15 , pp. 5230-5239
    • Höning, S.1    Griffith, J.2    Geuze, H.J.3    Hunziker, W.4
  • 56
    • 0032563130 scopus 로고    scopus 로고
    • Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network
    • Karlsson, K., Carlsson, S.R. Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network. J. Biol. Chem. 1998, 273, 18966-18973. [CrossRef] [PubMed]
    • (1998) J. Biol. Chem. , vol.273 , pp. 18966-18973
    • Karlsson, K.1    Carlsson, S.R.2
  • 58
    • 67349263394 scopus 로고    scopus 로고
    • Trafficking and function of the tetraspanin CD63
    • Pols, M.S., Klumperman, J. Trafficking and function of the tetraspanin CD63. Exp. Cell Res. 2009, 315, 1584-1592. [CrossRef] [PubMed]
    • (2009) Exp. Cell Res , vol.315 , pp. 1584-1592
    • Pols, M.S.1    Klumperman, J.2
  • 59
    • 79955010015 scopus 로고    scopus 로고
    • P-type lectins
    • Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds., Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA
    • Varki, A., Kornfeld, S. P-type lectins. In Essentials of Glycobiology, Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., Etzler, M.E., Eds., Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY, USA, 2009.
    • (2009) Essentials of Glycobiology
    • Varki, A.1    Kornfeld, S.2
  • 60
    • 70349882101 scopus 로고    scopus 로고
    • Carbohydrate recognition by the mannose-6-phosphate receptors
    • Kim, J.-J.P., Olson, L.J., Dahms, N.M. Carbohydrate recognition by the mannose-6-phosphate receptors. Curr. Opin. Struct. Biol. 2009, 19, 534-542. [CrossRef] [PubMed]
    • (2009) Curr. Opin. Struct. Biol , vol.19 , pp. 534-542
    • Kim, J.-J.P.1    Olson, L.J.2    Dahms, N.M.3
  • 61
    • 68149132035 scopus 로고    scopus 로고
    • Glycosylation-and phosphorylation-dependent intracellular transport of lysosomal hydrolases
    • Pohl, S., Marschner, K., Storch, S., Braulke, T. Glycosylation-and phosphorylation-dependent intracellular transport of lysosomal hydrolases. Biol. Chem. 2009, 390, 521-527. [CrossRef] [PubMed]
    • (2009) Biol. Chem , vol.390 , pp. 521-527
    • Pohl, S.1    Marschner, K.2    Storch, S.3    Braulke, T.4
  • 62
    • 0001261457 scopus 로고    scopus 로고
    • I-cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization
    • Schriver, C.R., Baudet, A.L., Sly, W.S., Valle, D., Eds., McGraw-Hill: New-York, NY, USA
    • Kornfeld, S., Sly, W.S. I-cell disease and pseudo-Hurler polydystrophy: Disorders of lysosomal enzyme phosphorylation and localization. In The Metabolic and Molecular Bases of Inherited Disease, Schriver, C.R., Baudet, A.L., Sly, W.S., Valle, D., Eds., McGraw-Hill: New-York, NY, USA, 2000.
    • (2000) The Metabolic and Molecular Bases of Inherited Disease
    • Kornfeld, S.1    Sly, W.S.2
  • 63
    • 84892347882 scopus 로고
    • Mucolipidosis II
    • Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J., Bird, T.D., Ledbetter, N., Mefford, H.C., Smith, R.J., et al., Eds., University ofWashington: Seattle, WA, USA
    • Leroy, J.G., Cathey, S., Friez, M.J. Mucolipidosis II. In GeneReviews®, Pagon, R.A., Adam, M.P., Ardinger, H.H., Wallace, S.E., Amemiya, A., Bean, L.J., Bird, T.D., Ledbetter, N., Mefford, H.C., Smith, R.J., et al., Eds., University ofWashington: Seattle, WA, USA, 1993.
    • (1993) GeneReviews®
    • Leroy, J.G.1    Cathey, S.2    Friez, M.J.3
  • 64
    • 0020411893 scopus 로고
    • Deficiency of UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients
    • Waheed, A., Pohlmann, R., Hasilik, A., von Figura, K., van Elsen, A., Leroy, J.G. Deficiency of UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients. Biochem. Biophys. Res. Commun. 1982, 105, 1052-1058. [CrossRef]
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 1052-1058
    • Waheed, A.1    Pohlmann, R.2    Hasilik, A.3    Von Figura, K.4    Van Elsen, A.5    Leroy, J.G.6
  • 65
    • 0020370152 scopus 로고
    • Is there a mechanism for introducing acid hydrolases into liver lysosomes that is independent of mannose 6-phosphate recognition? Evidence from I-cell disease
    • Owada, M., Neufeld, E.F. Is there a mechanism for introducing acid hydrolases into liver lysosomes that is independent of mannose 6-phosphate recognition? Evidence from I-cell disease. Biochem. Biophys. Res. Commun. 1982, 105, 814-820. [CrossRef]
    • (1982) Biochem. Biophys. Res. Commun , vol.105 , pp. 814-820
    • Owada, M.1    Neufeld, E.F.2
  • 67
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman, J.N., Kornfeld, S. Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell Biol. 1993, 123, 99-108. [CrossRef] [PubMed]
    • (1993) J. Cell Biol , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 68
    • 79954577494 scopus 로고    scopus 로고
    • Vacuolization of mucolipidosis type II mouse exocrine gland cells represents accumulation of autolysosomes
    • [PubMed]
    • Boonen, M., van Meel, E., Oorschot, V., Klumperman, J., Kornfeld, S. Vacuolization of mucolipidosis type II mouse exocrine gland cells represents accumulation of autolysosomes. Mol. Biol. Cell 2011, 22, 1135-1147. [CrossRef] [PubMed]
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1135-1147
    • Boonen, M.1    Van Meel, E.2    Oorschot, V.3    Klumperman, J.4    Kornfeld, S.5
  • 69
    • 79958765396 scopus 로고    scopus 로고
    • Disruption of the Man-6-P targeting pathway in mice impairs osteoclast secretory lysosome biogenesis
    • van Meel, E., Boonen, M., Zhao, H., Oorschot, V., Ross, F.P., Kornfeld, S., Klumperman, J. Disruption of the Man-6-P targeting pathway in mice impairs osteoclast secretory lysosome biogenesis. Traffic (Cph. Den.) 2011, 12, 912-924. [CrossRef] [PubMed]
    • (2011) Traffic (Cph. Den.) , vol.12 , pp. 912-924
    • Van Meel, E.1    Boonen, M.2    Zhao, H.3    Oorschot, V.4    Ross, F.P.5    Kornfeld, S.6    Klumperman, J.7
  • 72
    • 84907937915 scopus 로고    scopus 로고
    • Neurologic abnormalities in mouse models of the lysosomal storage disorders mucolipidosis II and mucolipidosis III
    • Idol, R.A., Wozniak, D.F., Fujiwara, H., Yuede, C.M., Ory, D.S., Kornfeld, S., Vogel, P. Neurologic abnormalities in mouse models of the lysosomal storage disorders mucolipidosis II and mucolipidosis III. PLoS ONE 2014, 9, e109768. [CrossRef] [PubMed]
    • (2014) Plos ONE , vol.9
    • Idol, R.A.1    Wozniak, D.F.2    Fujiwara, H.3    Yuede, C.M.4    Ory, D.S.5    Kornfeld, S.6    Vogel, P.7
  • 73
    • 0032980298 scopus 로고    scopus 로고
    • Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific
    • Dittmer, F., Ulbrich, E.J., Hafner, A., Schmahl, W., Meister, T., Pohlmann, R., von Figura, K. Alternative mechanisms for trafficking of lysosomal enzymes in mannose 6-phosphate receptor-deficient mice are cell type-specific. J. Cell Sci. 1999, 112 Pt 10, 1591-1597. [PubMed]
    • (1999) J. Cell Sci , vol.112 , pp. 1591-1597
    • Dittmer, F.1    Ulbrich, E.J.2    Hafner, A.3    Schmahl, W.4    Meister, T.5    Pohlmann, R.6    Von Figura, K.7
  • 74
    • 0036685345 scopus 로고    scopus 로고
    • Lysosome-associated protein transmembrane 4 α (LAPTM4 α) requires two tandemly arranged tyrosine-based signals for sorting to lysosomes
    • Hogue, D.L., Nash, C., Ling, V., Hobman, T.C. Lysosome-associated protein transmembrane 4 α (LAPTM4 α) requires two tandemly arranged tyrosine-based signals for sorting to lysosomes. Biochem. J. 2002, 365, 721-730. [CrossRef] [PubMed]
    • (2002) Biochem. J , vol.365 , pp. 721-730
    • Hogue, D.L.1    Nash, C.2    Ling, V.3    Hobman, T.C.4
  • 75
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor
    • Dell’Angelica, E.C., Shotelersuk, V., Aguilar, R.C., Gahl, W.A., Bonifacino, J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the β3A subunit of the AP-3 adaptor. Mol. Cell 1999, 3, 11-21. [CrossRef]
    • (1999) Mol. Cell , vol.3 , pp. 11-21
    • Dell’Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 77
    • 0032784330 scopus 로고    scopus 로고
    • Characterization of a fourth adaptor-related protein complex
    • Hirst, J., Bright, N.A., Rous, B., Robinson, M.S. Characterization of a fourth adaptor-related protein complex. Mol. Biol. Cell 1999, 10, 2787-2802. [CrossRef] [PubMed]
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2787-2802
    • Hirst, J.1    Bright, N.A.2    Rous, B.3    Robinson, M.S.4
  • 78
    • 24344449035 scopus 로고    scopus 로고
    • Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins
    • Janvier, K., Bonifacino, J.S. Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins. Mol. Biol. Cell 2005, 16, 4231-4242. [CrossRef] [PubMed]
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4231-4242
    • Janvier, K.1    Bonifacino, J.S.2
  • 79
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein lgp120 (Lgp-A) to lysosomes does not require appearance on the plasma membrane
    • Harter, C., Mellman, I. Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 1992, 117, 311-325. [CrossRef] [PubMed]
    • (1992) J. Cell Biol , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 80
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer, J., Schweizer, A., Russell, D., Kornfeld, S. The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J. Cell Biol. 1996, 132, 565-576. [CrossRef] [PubMed]
    • (1996) J. Cell Biol , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 81
    • 0036153670 scopus 로고    scopus 로고
    • The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes
    • Obermüller, S., Kiecke, C., von Figura, K., Höning, S. The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes. J. Cell Sci. 2002, 115, 185-194. [PubMed]
    • (2002) J. Cell Sci , vol.115 , pp. 185-194
    • Obermüller, S.1    Kiecke, C.2    Von Figura, K.3    Höning, S.4
  • 82
    • 1842509099 scopus 로고    scopus 로고
    • Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins
    • Peden, A.A., Oorschot, V., Hesser, B.A., Austin, C.D., Scheller, R.H., Klumperman, J. Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins. J. Cell Biol. 2004, 164, 1065-1076. [CrossRef] [PubMed]
    • (2004) J. Cell Biol , vol.164 , pp. 1065-1076
    • Peden, A.A.1    Oorschot, V.2    Hesser, B.A.3    Austin, C.D.4    Scheller, R.H.5    Klumperman, J.6
  • 83
    • 46349107378 scopus 로고    scopus 로고
    • AP-1 and AP-3 mediate sorting of melanosomal and lysosomal membrane proteins into distinct post-Golgi trafficking pathways
    • Chapuy, B., Tikkanen, R., Mühlhausen, C., Wenzel, D., von Figura, K., Höning, S. AP-1 and AP-3 mediate sorting of melanosomal and lysosomal membrane proteins into distinct post-Golgi trafficking pathways. Traffic (Cph. Den.) 2008, 9, 1157-1172. [CrossRef] [PubMed]
    • (2008) Traffic (Cph. Den.) , vol.9 , pp. 1157-1172
    • Chapuy, B.1    Tikkanen, R.2    Mühlhausen, C.3    Wenzel, D.4    Von Figura, K.5    Höning, S.6
  • 85
    • 0345732689 scopus 로고    scopus 로고
    • The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin
    • Lefrancois, S., Zeng, J., Hassan, A.J., Canuel, M., Morales, C.R. The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin. EMBO J. 2003, 22, 6430-6437. [CrossRef] [PubMed]
    • (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
  • 86
    • 37549057671 scopus 로고    scopus 로고
    • AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes
    • Canuel, M., Lefrancois, S., Zeng, J., Morales, C.R. AP-1 and retromer play opposite roles in the trafficking of sortilin between the Golgi apparatus and the lysosomes. Biochem. Biophys. Res. Commun. 2008, 366, 724-730. [CrossRef] [PubMed]
    • (2008) Biochem. Biophys. Res. Commun , vol.366 , pp. 724-730
    • Canuel, M.1    Lefrancois, S.2    Zeng, J.3    Morales, C.R.4
  • 87
    • 0035341211 scopus 로고    scopus 로고
    • The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein
    • Nielsen, M.S., Madsen, P., Christensen, E.I., Nykjaer, A., Gliemann, J., Kasper, D., Pohlmann, R., Petersen, C.M. The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein. EMBO J. 2001, 20, 2180-2190. [CrossRef] [PubMed]
    • (2001) EMBO J , vol.20 , pp. 2180-2190
    • Nielsen, M.S.1    Madsen, P.2    Christensen, E.I.3    Nykjaer, A.4    Gliemann, J.5    Kasper, D.6    Pohlmann, R.7    Petersen, C.M.8
  • 88
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu, H., Katoh, Y., Shiba, Y., Nakayama, K. Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 2001, 276, 28541-28545. [CrossRef] [PubMed]
    • (2001) J. Biol. Chem , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 89
    • 4143050395 scopus 로고    scopus 로고
    • The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins
    • Hassan, A.J., Zeng, J., Ni, X., Morales, C.R. The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of TM4 Sertoli cells is mediated by sortilin and monomeric adaptor proteins. Mol. Reprod. Dev. 2004, 68, 476-483. [CrossRef] [PubMed]
    • (2004) Mol. Reprod. Dev , vol.68 , pp. 476-483
    • Hassan, A.J.1    Zeng, J.2    Ni, X.3    Morales, C.R.4
  • 90
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • Le Borgne, R., Alconada, A., Bauer, U., Hoflack, B. The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J. Biol. Chem. 1998, 273, 29451-29461. [CrossRef] [PubMed]
    • (1998) J. Biol. Chem , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 91
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • Höning, S., Sandoval, I.V., von Figura, K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J. 1998, 17, 1304-1314. [CrossRef] [PubMed]
    • (1998) EMBO J , vol.17 , pp. 1304-1314
    • Höning, S.1    Sandoval, I.V.2    Von Figura, K.3
  • 92
    • 0033524994 scopus 로고    scopus 로고
    • In vitro binding study of adaptor protein complex (AP-1) to lysosomal targeting motif (LI-motif)
    • Fujita, H., Saeki, M., Yasunaga, K., Ueda, T., Imoto, T., Himeno, M. In vitro binding study of adaptor protein complex (AP-1) to lysosomal targeting motif (LI-motif). Biochem. Biophys. Res. Commun. 1999, 255, 54-58. [CrossRef] [PubMed]
    • (1999) Biochem. Biophys. Res. Commun , vol.255 , pp. 54-58
    • Fujita, H.1    Saeki, M.2    Yasunaga, K.3    Ueda, T.4    Imoto, T.5    Himeno, M.6
  • 93
    • 0034643282 scopus 로고    scopus 로고
    • Two acidic amino acid residues, Asp(470) and Glu(471), contained in the carboxyl cytoplasmic tail of a major lysosomal membrane protein, LGP85/LIMP II, are important for its accumulation in secondary lysosomes
    • Tabuchi, N., Akasaki, K., Tsuji, H. Two acidic amino acid residues, Asp(470) and Glu(471), contained in the carboxyl cytoplasmic tail of a major lysosomal membrane protein, LGP85/LIMP II, are important for its accumulation in secondary lysosomes. Biochem. Biophys. Res. Commun. 2000, 270, 557-563. [CrossRef] [PubMed]
    • (2000) Biochem. Biophys. Res. Commun , vol.270 , pp. 557-563
    • Tabuchi, N.1    Akasaki, K.2    Tsuji, H.3
  • 94
    • 0036305313 scopus 로고    scopus 로고
    • (476), a constituent of di-leucine-based motif of a major lysosomal membrane protein, LGP85/LIMP II, is important for its proper distribution in late endosomes and lysosomes
    • Tabuchi, N., Akasaki, K., Tsuji, H. Ile (476), a constituent of di-leucine-based motif of a major lysosomal membrane protein, LGP85/LIMP II, is important for its proper distribution in late endosomes and lysosomes. Biochem. Biophys. Res. Commun. 2002, 295, 149-156. [CrossRef]
    • (2002) Biochem. Biophys. Res. Commun , vol.295 , pp. 149-156
    • Tabuchi, N.1    Akasaki, K.2    Tsuji, H.I.3
  • 95
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1-sigma1 and AP-3 δ/σ3 hemicomplexes
    • Janvier, K., Kato, Y., Boehm, M., Rose, J.R., Martina, J.A., Kim, B.-Y., Venkatesan, S., Bonifacino, J.S. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1-sigma1 and AP-3 δ/σ3 hemicomplexes. J. Cell Biol. 2003, 163, 1281-1290. [CrossRef] [PubMed]
    • (2003) J. Cell Biol , vol.163 , pp. 1281-1290
    • Janvier, K.1    Kato, Y.2    Boehm, M.3    Rose, J.R.4    Martina, J.A.5    Kim, B.-Y.6    Venkatesan, S.7    Bonifacino, J.S.8
  • 96
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen, W.J., Goldstein, J.L., Brown, M.S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 1990, 265, 3116-3123. [PubMed]
    • (1990) J. Biol. Chem , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 98
    • 0036897341 scopus 로고    scopus 로고
    • Restoration of LDL receptor function in cells from patients with autosomal recessive hypercholesterolemia by retroviral expression of ARH1
    • Eden, E.R., Patel, D.D., Sun, X.-M., Burden, J.J., Themis, M., Edwards, M., Lee, P., Neuwirth, C., Naoumova, R.P., Soutar, A.K. Restoration of LDL receptor function in cells from patients with autosomal recessive hypercholesterolemia by retroviral expression of ARH1. J. Clin. Investig. 2002, 110, 1695-1702. [CrossRef] [PubMed]
    • (2002) J. Clin. Investig , vol.110 , pp. 1695-1702
    • Eden, E.R.1    Patel, D.D.2    Sun, X.-M.3    Burden, J.J.4    Themis, M.5    Edwards, M.6    Lee, P.7    Neuwirth, C.8    Naoumova, R.P.9    Soutar, A.K.10
  • 99
    • 0036668808 scopus 로고    scopus 로고
    • The mu2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and YppØ sorting signals at distinct sites
    • Boll, W., Rapoport, I., Brunner, C., Modis, Y., Prehn, S., Kirchhausen, T. The mu2 subunit of the clathrin adaptor AP-2 binds to FDNPVY and YppØ sorting signals at distinct sites. Traffic (Cph. Den.) 2002, 3, 590-600. [CrossRef]
    • (2002) Traffic (Cph. Den.) , vol.3 , pp. 590-600
    • Boll, W.1    Rapoport, I.2    Brunner, C.3    Modis, Y.4    Prehn, S.5    Kirchhausen, T.6
  • 100
    • 0034595799 scopus 로고    scopus 로고
    • The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein
    • Li, Y., Marzolo, M.P., van Kerkhof, P., Strous, G.J., Bu, G. The YXXL motif, but not the two NPXY motifs, serves as the dominant endocytosis signal for low density lipoprotein receptor-related protein. J. Biol. Chem. 2000, 275, 17187-17194. [CrossRef] [PubMed]
    • (2000) J. Biol. Chem , vol.275 , pp. 17187-17194
    • Li, Y.1    Marzolo, M.P.2    Van Kerkhof, P.3    Strous, G.J.4    Bu, G.5
  • 101
    • 70949087099 scopus 로고    scopus 로고
    • Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1
    • Guttman, M., Betts, G.N., Barnes, H., Ghassemian, M., van der Geer, P., Komives, E.A. Interactions of the NPXY microdomains of the low density lipoprotein receptor-related protein 1. Proteomics 2009, 9, 5016-5028. [CrossRef] [PubMed]
    • (2009) Proteomics , vol.9 , pp. 5016-5028
    • Guttman, M.1    Betts, G.N.2    Barnes, H.3    Ghassemian, M.4    Van Der Geer, P.5    Komives, E.A.6
  • 102
    • 0034193309 scopus 로고    scopus 로고
    • Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin
    • Oleinikov, A.V., Zhao, J., Makker, S.P. Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin. Biochem. J. 2000, 347 Pt 3, 613-621. [CrossRef] [PubMed]
    • (2000) Biochem. J , vol.347 , pp. 613-621
    • Oleinikov, A.V.1    Zhao, J.2    Makker, S.P.3
  • 103
    • 0037404459 scopus 로고    scopus 로고
    • Identification of an apical sorting determinant in the cytoplasmic tail of megalin
    • Takeda, T., Yamazaki, H., Farquhar, M.G. Identification of an apical sorting determinant in the cytoplasmic tail of megalin. Am. J. Physiol. Cell Physiol. 2003, 284, C1105-C1113. [CrossRef] [PubMed]
    • (2003) Am. J. Physiol. Cell Physiol , vol.284 , pp. C1105-C1113
    • Takeda, T.1    Yamazaki, H.2    Farquhar, M.G.3
  • 104
    • 0344875494 scopus 로고    scopus 로고
    • The adaptor protein ARH escorts megalin to and through endosomes
    • Nagai, M., Meerloo, T., Takeda, T., Farquhar, M.G. The adaptor protein ARH escorts megalin to and through endosomes. Mol. Biol. Cell 2003, 14, 4984-4996. [CrossRef] [PubMed]
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4984-4996
    • Nagai, M.1    Meerloo, T.2    Takeda, T.3    Farquhar, M.G.4
  • 105
    • 84957627541 scopus 로고    scopus 로고
    • Cathepsin D and its newly identified transport receptor SEZ6L2 can modulate neurite outgrowth
    • Boonen, M., Staudt, C., Gilis, F., Oorschot, V., Klumperman, J., Jadot, M. Cathepsin D and its newly identified transport receptor SEZ6L2 can modulate neurite outgrowth. J. Cell Sci. 2016, 129, 557-568. [CrossRef] [PubMed]
    • (2016) J. Cell Sci , vol.129 , pp. 557-568
    • Boonen, M.1    Staudt, C.2    Gilis, F.3    Oorschot, V.4    Klumperman, J.5    Jadot, M.6
  • 106
    • 0037136405 scopus 로고    scopus 로고
    • The mannose receptor family
    • East, L., Isacke, C.M. The mannose receptor family. Biochim. Biophys. Acta 2002, 1572, 364-386. [CrossRef]
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 364-386
    • East, L.1    Isacke, C.M.2
  • 107
    • 0026481131 scopus 로고
    • Phagocytic chimeric receptors require both transmembrane and cytoplasmic domains from the mannose receptor
    • Kruskal, B.A., Sastry, K., Warner, A.B., Mathieu, C.E., Ezekowitz, R.A. Phagocytic chimeric receptors require both transmembrane and cytoplasmic domains from the mannose receptor. J. Exp. Med. 1992, 176, 1673-1680. [CrossRef] [PubMed]
    • (1992) J. Exp. Med , vol.176 , pp. 1673-1680
    • Kruskal, B.A.1    Sastry, K.2    Warner, A.B.3    Mathieu, C.E.4    Ezekowitz, R.A.5
  • 111
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: Understanding the endo-lysosomal system
    • van Meel, E., Klumperman, J. Imaging and imagination: Understanding the endo-lysosomal system. Histochem. Cell Biol. 2008, 129, 253-266. [CrossRef] [PubMed]
    • (2008) Histochem. Cell Biol , vol.129 , pp. 253-266
    • Van Meel, E.1    Klumperman, J.2
  • 112
    • 84858698808 scopus 로고    scopus 로고
    • Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction
    • Coutinho, M.F., Prata, M.J., Alves, S. Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction. Mol. Genet. Metab. 2012, 105, 542-550. [CrossRef] [PubMed]
    • (2012) Mol. Genet. Metab , vol.105 , pp. 542-550
    • Coutinho, M.F.1    Prata, M.J.2    Alves, S.3
  • 114
    • 1842866714 scopus 로고    scopus 로고
    • Role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology
    • Kuronita, T., Eskelinen, E.-L., Fujita, H., Saftig, P., Himeno, M., Tanaka, Y. A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology. J. Cell Sci. 2002, 115, 4117-4131. [CrossRef] [PubMed]
    • (2002) J. Cell Sci , vol.115 , pp. 4117-4131
    • Kuronita, T.1    Eskelinen, E.-L.2    Fujita, H.3    Saftig, P.4    Himeno, M.5    Tanaka, Y.A.6
  • 116
    • 33745022321 scopus 로고    scopus 로고
    • The lysosomal trafficking of acid sphingomyelinase is mediated by sortilin and mannose 6-phosphate receptor
    • Ni, X., Morales, C.R. The lysosomal trafficking of acid sphingomyelinase is mediated by sortilin and mannose 6-phosphate receptor. Traffic (Cph. Den.) 2006, 7, 889-902. [CrossRef] [PubMed]
    • (2006) Traffic (Cph. Den.) , vol.7 , pp. 889-902
    • Ni, X.1    Morales, C.R.2
  • 118
    • 70349785144 scopus 로고    scopus 로고
    • The inactivation of the sortilin gene leads to a partial disruption of prosaposin trafficking to the lysosomes
    • Zeng, J., Racicott, J., Morales, C.R. The inactivation of the sortilin gene leads to a partial disruption of prosaposin trafficking to the lysosomes. Exp. Cell Res. 2009, 315, 3112-3124. [CrossRef] [PubMed]
    • (2009) Exp. Cell Res , vol.315 , pp. 3112-3124
    • Zeng, J.1    Racicott, J.2    Morales, C.R.3
  • 119
    • 63449103189 scopus 로고    scopus 로고
    • The interactomics of sortilin: An ancient lysosomal receptor evolving new functions
    • Canuel, M., Libin, Y., Morales, C.R. The interactomics of sortilin: An ancient lysosomal receptor evolving new functions. Histol. Histopathol. 2009, 24, 481-492. [PubMed]
    • (2009) Histol. Histopathol , vol.24 , pp. 481-492
    • Canuel, M.1    Libin, Y.2    Morales, C.R.3
  • 120
    • 77954898687 scopus 로고    scopus 로고
    • Gutierrez, M.G. Golgi-to-phagosome transport of acid sphingomyelinase and prosaposin is mediated by sortilin
    • Wähe, A., Kasmapour, B., Schmaderer, C., Liebl, D., Sandhoff, K., Nykjaer, A., Griffiths, G., Gutierrez, M.G. Golgi-to-phagosome transport of acid sphingomyelinase and prosaposin is mediated by sortilin. J. Cell Sci. 2010, 123, 2502-2511. [CrossRef] [PubMed]
    • (2010) J. Cell Sci , vol.123 , pp. 2502-2511
    • Wähe, A.1    Kasmapour, B.2    Schmaderer, C.3    Liebl, D.4    Sandhoff, K.5    Nykjaer, A.6    Griffiths, G.7
  • 122
    • 33947201045 scopus 로고    scopus 로고
    • Distribution of α-galactosidase A in normal human kidney and renal accumulation and distribution of recombinant alpha-galactosidase A in Fabry mice
    • Christensen, E.I., Zhou, Q., Sørensen, S.S., Rasmussen, A.K., Jacobsen, C., Feldt-Rasmussen, U., Nielsen, R. Distribution of α-galactosidase A in normal human kidney and renal accumulation and distribution of recombinant alpha-galactosidase A in Fabry mice. J. Am. Soc. Nephrol. JASN 2007, 18, 698-706. [CrossRef] [PubMed]
    • (2007) J. Am. Soc. Nephrol. JASN , vol.18 , pp. 698-706
    • Christensen, E.I.1    Zhou, Q.2    Sørensen, S.S.3    Rasmussen, A.K.4    Jacobsen, C.5    Feldt-Rasmussen, U.6    Nielsen, R.7
  • 125
    • 84863227600 scopus 로고    scopus 로고
    • Cathepsin D is partly endocytosed by the LRP1 receptor and inhibits LRP1-regulated intramembrane proteolysis
    • Derocq, D., Prébois, C., Beaujouin, M., Laurent-Matha, V., Pattingre, S., Smith, G.K., Liaudet-Coopman, E. Cathepsin D is partly endocytosed by the LRP1 receptor and inhibits LRP1-regulated intramembrane proteolysis. Oncogene 2012, 31, 3202-3212. [CrossRef] [PubMed]
    • (2012) Oncogene , vol.31 , pp. 3202-3212
    • Derocq, D.1    Prébois, C.2    Beaujouin, M.3    Laurent-Matha, V.4    Pattingre, S.5    Smith, G.K.6    Liaudet-Coopman, E.7
  • 127
    • 0031709904 scopus 로고    scopus 로고
    • Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors
    • Laurent-Matha, V., Farnoud, M.R., Lucas, A., Rougeot, C., Garcia, M., Rochefort, H. Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors. J. Cell Sci. 1998, 111 Pt 17, 2539-2549. [PubMed]
    • (1998) J. Cell Sci , vol.111 , pp. 2539-2549
    • Laurent-Matha, V.1    Farnoud, M.R.2    Lucas, A.3    Rougeot, C.4    Garcia, M.5    Rochefort, H.6
  • 128
    • 84876263985 scopus 로고    scopus 로고
    • Systematic proteomic analysis identifies β-site amyloid precursor protein cleaving enzyme 2 and 1 (BACE2 and BACE1) substrates in pancreatic β-cells
    • Stützer, I., Selevsek, N., Esterházy, D., Schmidt, A., Aebersold, R., Stoffel, M. Systematic proteomic analysis identifies β-site amyloid precursor protein cleaving enzyme 2 and 1 (BACE2 and BACE1) substrates in pancreatic β-cells. J. Biol. Chem. 2013, 288, 10536-10547. [CrossRef] [PubMed]
    • (2013) J. Biol. Chem , vol.288 , pp. 10536-10547
    • Stützer, I.1    Selevsek, N.2    Esterházy, D.3    Schmidt, A.4    Aebersold, R.5    Stoffel, M.6
  • 130
    • 33745844760 scopus 로고    scopus 로고
    • Disturbance of cerebellar synaptic maturation in mutant mice lacking BSRPs, a novel brain-specific receptor-like protein family
    • Miyazaki, T., Hashimoto, K., Uda, A., Sakagami, H., Nakamura, Y., Saito, S., Nishi, M., Kume, H., Tohgo, A., Kaneko, I., et al. Disturbance of cerebellar synaptic maturation in mutant mice lacking BSRPs, a novel brain-specific receptor-like protein family. FEBS Lett. 2006, 580, 4057-4064. [CrossRef] [PubMed]
    • (2006) FEBS Lett , vol.580 , pp. 4057-4064
    • Miyazaki, T.1    Hashimoto, K.2    Uda, A.3    Sakagami, H.4    Nakamura, Y.5    Saito, S.6    Nishi, M.7    Kume, H.8    Tohgo, A.9    Kaneko, I.10
  • 132
    • 0018170526 scopus 로고
    • Sly,W.S. Human beta-glucuronidase: In vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells
    • Achord, D.T., Brot, F.E., Bell, C.E., Sly,W.S. Human beta-glucuronidase: In vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells. Cell 1978, 15, 269-278. [CrossRef]
    • (1978) Cell , vol.15 , pp. 269-278
    • Achord, D.T.1    Brot, F.E.2    Bell, C.E.3
  • 133
    • 0018634472 scopus 로고
    • An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver. I. Distribution of 125I-ligands among the liver cell types
    • Hubbard, A.L., Wilson, G., Ashwell, G., Stukenbrok, H. An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver. I. Distribution of 125I-ligands among the liver cell types. J. Cell Biol. 1979, 83, 47-64. [CrossRef] [PubMed]
    • (1979) J. Cell Biol , vol.83 , pp. 47-64
    • Hubbard, A.L.1    Wilson, G.2    Ashwell, G.3    Stukenbrok, H.4
  • 134
    • 0019784197 scopus 로고
    • Oligosaccharide specific endocytosis by isolated rat hepatic reticuloendothelial cells
    • Maynard, Y., Baenziger, J.U. Oligosaccharide specific endocytosis by isolated rat hepatic reticuloendothelial cells. J. Biol. Chem. 1981, 256, 8063-8068. [PubMed]
    • (1981) J. Biol. Chem , vol.256 , pp. 8063-8068
    • Maynard, Y.1    Baenziger, J.U.2
  • 135
    • 0023388925 scopus 로고
    • Isolation and characterization of a mannose-specific endocytosis receptor from rabbit alveolar macrophages
    • Lennartz, M.R., Wileman, T.E., Stahl, P.D. Isolation and characterization of a mannose-specific endocytosis receptor from rabbit alveolar macrophages. Biochem. J. 1987, 245, 705-711. [CrossRef] [PubMed]
    • (1987) Biochem. J , vol.245 , pp. 705-711
    • Lennartz, M.R.1    Wileman, T.E.2    Stahl, P.D.3
  • 136
    • 0025362207 scopus 로고
    • Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains
    • Taylor, M.E., Conary, J.T., Lennartz, M.R., Stahl, P.D., Drickamer, K. Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains. J. Biol. Chem. 1990, 265, 12156-12162. [PubMed]
    • (1990) J. Biol. Chem , vol.265 , pp. 12156-12162
    • Taylor, M.E.1    Conary, J.T.2    Lennartz, M.R.3    Stahl, P.D.4    Drickamer, K.5
  • 138
    • 58149399414 scopus 로고    scopus 로고
    • Liver sinusoidal endothelial cells depend on mannose receptor-mediated recruitment of lysosomal enzymes for normal degradation capacity
    • Elvevold, K., Simon-Santamaria, J., Hasvold, H., McCourt, P., Smedsrød, B., Sørensen, K.K. Liver sinusoidal endothelial cells depend on mannose receptor-mediated recruitment of lysosomal enzymes for normal degradation capacity. Hepatology 2008, 48, 2007-2015. [CrossRef] [PubMed]
    • (2008) Hepatology , vol.48 , pp. 2007-2015
    • Elvevold, K.1    Simon-Santamaria, J.2    Hasvold, H.3    McCourt, P.4    Smedsrød, B.5    Sørensen, K.K.6
  • 140
    • 84897559750 scopus 로고    scopus 로고
    • Subcellular trafficking and activity of Hyal-1 and its processed forms in murine macrophages
    • Puissant, E., Gilis, F., Dogné, S., Flamion, B., Jadot, M., Boonen, M. Subcellular trafficking and activity of Hyal-1 and its processed forms in murine macrophages. Traffic (Cph. Den.) 2014, 15, 500-515. [CrossRef] [PubMed]
    • (2014) Traffic (Cph. Den.) , vol.15 , pp. 500-515
    • Puissant, E.1    Gilis, F.2    Dogné, S.3    Flamion, B.4    Jadot, M.5    Boonen, M.6
  • 141
    • 84899486635 scopus 로고    scopus 로고
    • Mouse liver lysosomes contain enzymatically active processed forms of Hyal-1. Biochem. Biophys. Res
    • Boonen, M., Puissant, E., Gilis, F., Flamion, B., Jadot, M. Mouse liver lysosomes contain enzymatically active processed forms of Hyal-1. Biochem. Biophys. Res. Commun. 2014, 446, 1155-1160. [CrossRef] [PubMed]
    • (2014) Commun , vol.446 , pp. 1155-1160
    • Boonen, M.1    Puissant, E.2    Gilis, F.3    Flamion, B.4    Jadot, M.5
  • 142
    • 0019475525 scopus 로고
    • Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation
    • Furbish, F.S., Steer, C.J., Krett, N.L., Barranger, J.A. Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation. Biochim. Biophys. Acta 1981, 673, 425-434. [CrossRef]
    • (1981) Biochim. Biophys. Acta , vol.673 , pp. 425-434
    • Furbish, F.S.1    Steer, C.J.2    Krett, N.L.3    Barranger, J.A.4
  • 143
    • 0028018009 scopus 로고
    • Modifying exogenous glucocerebrosidase for effective replacement therapy in Gaucher disease
    • Brady, R.O., Murray, G.J., Barton, N.W. Modifying exogenous glucocerebrosidase for effective replacement therapy in Gaucher disease. J. Inherit. Metab. Dis. 1994, 17, 510-519. [CrossRef] [PubMed]
    • (1994) J. Inherit. Metab. Dis , vol.17 , pp. 510-519
    • Brady, R.O.1    Murray, G.J.2    Barton, N.W.3
  • 144
    • 84992315783 scopus 로고    scopus 로고
    • Monocytes/macrophages upregulate the hyaluronidase HYAL1 and adapt its subcellular trafficking to promote extracellular residency upon differentiation into osteoclasts
    • Puissant, E., Boonen, M. Monocytes/macrophages upregulate the hyaluronidase HYAL1 and adapt its subcellular trafficking to promote extracellular residency upon differentiation into osteoclasts. PLoS ONE 2016, 11, e0165004. [CrossRef] [PubMed]
    • (2016) Plos ONE , vol.11
    • Puissant, E.1    Boonen, M.2
  • 145
    • 84907546604 scopus 로고    scopus 로고
    • Molecular characterization of arylsulfatase G: Expression, processing, glycosylation, transport, and activity
    • Kowalewski, B., Lübke, T., Kollmann, K., Braulke, T., Reinheckel, T., Dierks, T., Damme, M. Molecular characterization of arylsulfatase G: Expression, processing, glycosylation, transport, and activity. J. Biol. Chem. 2014, 289, 27992-28005. [CrossRef] [PubMed]
    • (2014) J. Biol. Chem , vol.289 , pp. 27992-28005
    • Kowalewski, B.1    Lübke, T.2    Kollmann, K.3    Braulke, T.4    Reinheckel, T.5    Dierks, T.6    Damme, M.7
  • 146
    • 0023784539 scopus 로고
    • Intracellular transport of acid _-glucosidase in human fibroblasts: Evidence for involvement of phosphomannosyl receptor-independent system
    • Tsuji, A., Omura, K., Suzuki, Y. Intracellular transport of acid _-glucosidase in human fibroblasts: Evidence for involvement of phosphomannosyl receptor-independent system. J. Biochem. (Tokyo) 1988, 104, 276-278. [PubMed]
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 276-278
    • Tsuji, A.1    Omura, K.2    Suzuki, Y.3
  • 147
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Díaz, E., Pfeffer, S.R. TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking. Cell 1998, 93, 433-443. [CrossRef]
    • (1998) Cell , vol.93 , pp. 433-443
    • Díaz, E.1    Pfeffer, S.R.2
  • 148
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • Carroll, K.S., Hanna, J., Simon, I., Krise, J., Barbero, P., Pfeffer, S.R. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science 2001, 292, 1373-1376. [CrossRef] [PubMed]
    • (2001) Science , vol.292 , pp. 1373-1376
    • Carroll, K.S.1    Hanna, J.2    Simon, I.3    Krise, J.4    Barbero, P.5    Pfeffer, S.R.6
  • 149
    • 84904860445 scopus 로고    scopus 로고
    • MTOR and lysosome regulation
    • Puertollano, R. mTOR and lysosome regulation. F1000prime Rep. 2014, 6, 52. [CrossRef] [PubMed]
    • (2014) F1000prime Rep , vol.6 , pp. 52
    • Puertollano, R.1
  • 150
    • 84865592978 scopus 로고    scopus 로고
    • Amino acids and mTORC1: From lysosomes to disease
    • Efeyan, A., Zoncu, R., Sabatini, D.M. Amino acids and mTORC1: From lysosomes to disease. Trends Mol. Med. 2012, 18, 524-533. [CrossRef] [PubMed]
    • (2012) Trends Mol. Med , vol.18 , pp. 524-533
    • Efeyan, A.1    Zoncu, R.2    Sabatini, D.M.3
  • 151
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., Sabatini, D.M. mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 2011, 334, 678-683. [CrossRef] [PubMed]
    • (2011) Science , vol.334 , pp. 678-683
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3    Wang, S.4    Sancak, Y.5    Sabatini, D.M.6
  • 152
    • 84946569689 scopus 로고    scopus 로고
    • Amino acid availability modulates vacuolar H+-ATPase assembly
    • Stransky, L.A., Forgac, M. Amino acid availability modulates vacuolar H+-ATPase assembly. J. Biol. Chem. 2015, 290, 27360-27369. [CrossRef] [PubMed]
    • (2015) J. Biol. Chem , vol.290 , pp. 27360-27369
    • Stransky, L.A.1    Forgac, M.2
  • 154
    • 84915793059 scopus 로고    scopus 로고
    • Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation
    • Chang, J., Lee, S., Blackstone, C. Spastic paraplegia proteins spastizin and spatacsin mediate autophagic lysosome reformation. J. Clin. Investig. 2014, 124, 5249-5262. [CrossRef] [PubMed]
    • (2014) J. Clin. Investig , vol.124 , pp. 5249-5262
    • Chang, J.1    Lee, S.2    Blackstone, C.3
  • 156
    • 79960745991 scopus 로고    scopus 로고
    • Unconventional secretion: A stress on GRASP
    • Giuliani, F., Grieve, A., Rabouille, C. Unconventional secretion: A stress on GRASP. Curr. Opin. Cell Biol. 2011, 23, 498-504. [CrossRef] [PubMed]
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 498-504
    • Giuliani, F.1    Grieve, A.2    Rabouille, C.3
  • 157
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W., Rabouille, C. Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 2009, 10, 148-155. [CrossRef] [PubMed]
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 158
    • 84864295258 scopus 로고    scopus 로고
    • Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation
    • Deretic, V., Jiang, S., Dupont, N. Autophagy intersections with conventional and unconventional secretion in tissue development, remodeling and inflammation. Trends Cell Biol. 2012, 22, 397-406. [CrossRef] [PubMed]
    • (2012) Trends Cell Biol , vol.22 , pp. 397-406
    • Deretic, V.1    Jiang, S.2    Dupont, N.3
  • 161
    • 84975818604 scopus 로고    scopus 로고
    • Molecular determinants that mediate the sorting of human ATG9A from the endoplasmic reticulum
    • Staudt, C., Gilis, F., Boonen, M., Jadot, M. Molecular determinants that mediate the sorting of human ATG9A from the endoplasmic reticulum. Biochim. Biophys. Acta 2016, 1863, 2299-2310. [CrossRef] [PubMed]
    • (2016) Biochim. Biophys. Acta , vol.1863 , pp. 2299-2310
    • Staudt, C.1    Gilis, F.2    Boonen, M.3    Jadot, M.4
  • 162
    • 70350632412 scopus 로고    scopus 로고
    • Secretory Golgi bypass route to the apical surface domain of epithelial MDCK cells
    • Tveit, H., Akslen, L.K.A., Fagereng, G.L., Tranulis, M.A., Prydz, K. A secretory Golgi bypass route to the apical surface domain of epithelial MDCK cells. Traffic (Cph. Den.) 2009, 10, 1685-1695. [CrossRef] [PubMed]
    • (2009) Traffic (Cph. Den.) , vol.10 , pp. 1685-1695
    • Tveit, H.1    Akslen, L.K.A.2    Fagereng, G.L.3    Tranulis, M.A.4    Prydz, K.A.5
  • 163
    • 70350509583 scopus 로고    scopus 로고
    • Successful treatment of the murine model of cystinosis using bone marrow cell transplantation
    • Syres, K., Harrison, F., Tadlock, M., Jester, J.V., Simpson, J., Roy, S., Salomon, D.R., Cherqui, S. Successful treatment of the murine model of cystinosis using bone marrow cell transplantation. Blood 2009, 114, 2542-2552. [CrossRef] [PubMed]
    • (2009) Blood , vol.114 , pp. 2542-2552
    • Syres, K.1    Harrison, F.2    Tadlock, M.3    Jester, J.V.4    Simpson, J.5    Roy, S.6    Salomon, D.R.7    Cherqui, S.8
  • 167
    • 1142286348 scopus 로고    scopus 로고
    • Nanotubular highways for intercellular organelle transport
    • Rustom, A., Saffrich, R., Markovic, I., Walther, P., Gerdes, H.-H. Nanotubular highways for intercellular organelle transport. Science 2004, 303, 1007-1010. [CrossRef] [PubMed]
    • (2004) Science , vol.303 , pp. 1007-1010
    • Rustom, A.1    Saffrich, R.2    Markovic, I.3    Walther, P.4    Gerdes, H.-H.5
  • 168
    • 84978280502 scopus 로고    scopus 로고
    • The missing link: Does tunnelling nanotube-based supercellularity provide a new understanding of chronic and lifestyle diseases?
    • Rustom, A. The missing link: Does tunnelling nanotube-based supercellularity provide a new understanding of chronic and lifestyle diseases? Open Biol. 2016, 6, 160057. [CrossRef] [PubMed]
    • (2016) Open Biol , vol.6
    • Rustom, A.1
  • 169
    • 84929506373 scopus 로고    scopus 로고
    • Ectosomes and exosomes: Shedding the confusion between extracellular vesicles
    • Cocucci, E., Meldolesi, J. Ectosomes and exosomes: Shedding the confusion between extracellular vesicles. Trends Cell Biol. 2015, 25, 364-372. [CrossRef] [PubMed]
    • (2015) Trends Cell Biol , vol.25 , pp. 364-372
    • Cocucci, E.1    Meldolesi, J.2
  • 172
    • 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., Sleat, D.E., Zheng, H., Moore, D., Lobel, P. Proteomics analysis of serum from mutant mice reveals lysosomal proteins selectively transported by each of the two mannose 6-phosphate receptors. Mol. Cell. Proteom. MCP 2008, 7, 58-70. [CrossRef] [PubMed]
    • (2008) Mol. Cell. Proteom. MCP , vol.7 , pp. 58-70
    • Qian, M.1    Sleat, D.E.2    Zheng, H.3    Moore, D.4    Lobel, P.5
  • 173
    • 0026577083 scopus 로고
    • Expression of the two mannose 6-phosphate receptors is spatially and temporally different during mouse embryogenesis
    • Matzner, U., von Figura, K., Pohlmann, R. Expression of the two mannose 6-phosphate receptors is spatially and temporally different during mouse embryogenesis. Development (Camb.) 1992, 114, 965-972.
    • (1992) Development (Camb.) , vol.114 , pp. 965-972
    • Matzner, U.1    Von Figura, K.2    Pohlmann, R.3
  • 175
    • 14844298698 scopus 로고    scopus 로고
    • Immunohistochemical distribution of cation-dependent mannose 6-phosphate receptors in the mouse central nervous system: Comparison with that of cation-independent mannose 6-phophate receptors. Neurosci
    • Konishi, Y., Fushimi, S., Shirabe, T. Immunohistochemical distribution of cation-dependent mannose 6-phosphate receptors in the mouse central nervous system: Comparison with that of cation-independent mannose 6-phophate receptors. Neurosci. Lett. 2005, 378, 7-12. [CrossRef] [PubMed]
    • (2005) Lett , vol.378 , pp. 7-12
    • Konishi, Y.1    Fushimi, S.2    Shirabe, T.3


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