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Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
Abstract
The cation-independent mannose 6-phosphate receptor (CI-MPR) mediates sorting of lysosomal hydrolase precursors from the TGN to endosomes. After releasing the hydrolase precursors into the endosomal lumen, the unoccupied receptor returns to the TGN for further rounds of sorting. Here, we show that the mammalian retromer complex participates in this retrieval pathway. The hVps35 subunit of retromer interacts with the cytosolic domain of the CI-MPR. This interaction probably occurs in an endosomal compartment, where most of the retromer is localized. In particular, retromer is associated with tubular–vesicular profiles that emanate from early endosomes or from intermediates in the maturation from early to late endosomes. Depletion of retromer by RNA interference increases the lysosomal turnover of the CI-MPR, decreases cellular levels of lysosomal hydrolases, and causes swelling of lysosomes. These observations indicate that retromer prevents the delivery of the CI-MPR to lysosomes, probably by sequestration into endosome-derived tubules from where the receptor returns to the TGN.
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The retromer recycles specific cargos including CI-MPR, which is involved in delivery of proteolytic enzymes to lysosomes.
“The retromer recycles specific cargos, such as Vps10/Sortilin protein family members14 or the cation-independent mannose 6-phosphate receptor (CI-MPR)15. The latter is involved in the delivery of proteolytic enzymes to lysosomes.”
From Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis (2020) · cites this paper as [15]
Many studies in mammalian cells are consistent with a role for retromer in CI-MPR transport.
“Many studies in mammalian cells are consistent with a role for retromer in CI-MPR transport (Arighi et al., 2004; Seaman, 2004, 2007; Wassmer et al., 2007; Bulankina et al., 2009; Harbour et al., 2010; Hao et al., 2013; Breusegem and Seaman, 2014; McGough et al., 2014; Cui et al., 2019).”
From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Arighi et al., 2004
Knockdown of a single CRC protein affects the expression of the other CRC members.
“Knockdown of a single CRC protein affects the expression of the other CRC members15,21.”
From Retromer stabilization results in neuroprotection in a model of Amyotrophic Lateral Sclerosis (2020) · cites this paper as [15]
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Cites
Raposo, G., Tenza, D., Murphy, D. M., Berson, J. F., & Marks, M. S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.809 · Cited by 451
Haft, C. R., de la Luz Sierra, M., Barr, V. A., Haft, D. H., & Taylor, S. I. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7278 · Cited by 244
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Research works printed but not linked: 74
- 2002, J. Cell Biol., 156, 511, 10.1083/jcb.200109030 · DOI
- 1997, Mol. Biol. Cell., 8, 1261, 10.1091/mbc.8.7.1261 · DOI
- 2002, EMBO J., 21, 2557, 10.1093/emboj/21.11.2557 · DOI · Paper page
- 1993, J. Biol. Chem., 268, 22338, 10.1016/S0021-9258(18)41533-5 · DOI
- 1997, J. Biol. Chem., 272, 7003, 10.1074/jbc.272.11.7003 · DOI
- 1996, J. Cell Biol., 133, 529, 10.1083/jcb.133.3.529 · DOI
- 2001, Mol. Biol. Cell., 12, 1885, 10.1091/mbc.12.6.1885 · DOI
- 1983, Biochem. J., 214, 353, 10.1042/bj2140353 · DOI
- 2000, J. Cell Biol., 149, 81, 10.1083/jcb.149.1.81 · DOI · Paper page
- 2001, Mol. Biol. Cell., 12, 475, 10.1091/mbc.12.2.475 · DOI
- 1998, Cell., 93, 433, 10.1016/S0092-8674(00)81171-X · DOI
- 1994, J. Biol. Chem., 269, 12159, 10.1016/S0021-9258(17)32695-9 · DOI
- 2002, Science., 297, 1700, 10.1126/science.1075327 · DOI · Paper page
- 1983, Eur. J. Cell Biol., 32, 38
- 1985, J. Cell Biol., 101, 2253, 10.1083/jcb.101.6.2253 · DOI
- 1988, J. Cell Biol., 107, 2491, 10.1083/jcb.107.6.2491 · DOI
- 2003, Nat. Rev. Mol. Cell Biol., 4, 202, 10.1038/nrm1050 · DOI
- 1989, EMBO J., 8, 1041, 10.1002/j.1460-2075.1989.tb03471.x · DOI
- 1989, J. Cell Biol., 109, 2703, 10.1083/jcb.109.6.2703 · DOI
- 2000, Mol. Biol. Cell., 11, 4105, 10.1091/mbc.11.12.4105 · DOI · Paper page
- 2003, EMBO J., 22, 548, 10.1093/emboj/cdg062 · DOI
- 1998, Mol. Biol. Cell., 9, 809, 10.1091/mbc.9.4.809 · DOI
- 2000, J. Cell Biol., 149, 67, 10.1083/jcb.149.1.67 · DOI · Paper page
- 2001, Mol. Biol. Cell., 12, 3573, 10.1091/mbc.12.11.3573 · DOI
- 1985, J. Biol. Chem., 260, 12008, 10.1016/S0021-9258(17)38977-9 · DOI
- 1997, J. Biol. Chem., 272, 19884, 10.1074/jbc.272.32.19884 · DOI
- 1983, Cell., 35, 321, 10.1016/0092-8674(83)90235-0 · DOI
- 1997, Mol. Biol. Cell., 8, 1529, 10.1091/mbc.8.8.1529 · DOI
- 1992, J. Biol. Chem., 267, 11069, 10.1016/S0021-9258(19)49876-1 · DOI
- 1992, J. Cell Biol., 119, 249, 10.1083/jcb.119.2.249 · DOI
- 1993, J. Cell Biol., 121, 997, 10.1083/jcb.121.5.997 · DOI
- 1998, J. Cell Biol., 141, 359, 10.1083/jcb.141.2.359 · DOI
- 1989, Annu. Rev. Cell Biol., 5, 483, 10.1146/annurev.cb.05.110189.002411 · DOI
- 2000, J. Biol. Chem., 275, 25188, 10.1074/jbc.M001138200 · DOI
- 1996, Science., 272, 1008, 10.1126/science.272.5264.1008 · DOI · Paper page
- 2001, J. Cell Sci., 114, 1743, 10.1242/jcs.114.9.1743 · DOI · Paper page
- 2004, Mol. Biol. Cell., 15, 721, 10.1091/mbc.e03-07-0497 · DOI
- 1991, J. Cell Biol., 115, 1561, 10.1083/jcb.115.6.1561 · DOI
- 1999, J. Cell Biol., 146, 345, 10.1083/jcb.146.2.345 · DOI
- 1994, Cell., 77, 579, 10.1016/0092-8674(94)90219-4 · DOI · Paper page
- 1996, J. Biol. Chem., 271, 2171, 10.1074/jbc.271.4.2171 · DOI
- 2000, EMBO J., 19, 2193, 10.1093/emboj/19.10.2193 · DOI · Paper page
- 2001, J. Cell Sci., 114, 4469, 10.1242/jcs.114.24.4469 · DOI · Paper page
- 2004, EMBO J., 23, 386, 10.1038/sj.emboj.7600041 · DOI · Paper page
- 2001, Mol. Cell. Biol., 21, 7981, 10.1128/MCB.21.23.7981-7994.2001 · DOI
- 1999, Mol. Biol. Cell., 10, 875, 10.1091/mbc.10.4.875 · DOI
- 2000, J. Cell Biol., 151, 297, 10.1083/jcb.151.2.297 · DOI
- 2000, Proc. Natl. Acad. Sci. USA., 97, 9047, 10.1073/pnas.160251397 · DOI
- 2004, Science., 303, 495, 10.1126/science.1092586 · DOI · Paper page
- 1998, J. Cell Biol., 140, 1075, 10.1083/jcb.140.5.1075 · DOI
- 2001, Science., 292, 1712, 10.1126/science.1060750 · DOI · Paper page
- 2003, Mol. Biol. Cell., 14, 1545, 10.1091/mbc.02-07-0109 · DOI
- 2002, Nat. Cell Biol., 4, 394, 10.1038/ncb791 · DOI · Paper page
- 2003, Curr Opin. Cell Biol., 15, 446, 10.1016/S0955-0674(03)00080-2 · DOI
- 2001, Mol. Biol. Cell., 12, 3242, 10.1091/mbc.12.10.3242 · DOI
- 1992, J. Biol. Chem., 267, 15665, 10.1016/S0021-9258(19)49587-2 · DOI
- 1995, J. Cell Biol., 130, 1297, 10.1083/jcb.130.6.1297 · DOI
- 1991, J. Biol. Chem., 266, 22557, 10.1016/S0021-9258(18)54608-1 · DOI
- 2002, Mol. Biol. Cell., 13, 1313, 10.1091/mbc.01-10-0525 · DOI · Paper page
- 1981, Proc. Natl. Acad. Sci. USA., 78, 4289, 10.1073/pnas.78.7.4289 · DOI
- 2002, Mol. Biol. Cell., 13, 2826, 10.1091/mbc.02-05-0064 · DOI · Paper page
- 1997, J. Cell Biol., 137, 79, 10.1083/jcb.137.1.79 · DOI · Paper page
- 1998, J. Cell Biol., 142, 665, 10.1083/jcb.142.3.665 · DOI · Paper page
- 1992, EMBO J., 11, 2811, 10.1002/j.1460-2075.1992.tb05348.x · DOI · Paper page
- 1994, EMBO J., 13, 1287, 10.1002/j.1460-2075.1994.tb06381.x · DOI · Paper page
- 2001, J. Biol. Chem., 276, 28541, 10.1074/jbc.C100218200 · DOI
- 1998, J. Cell Sci., 111, 877, 10.1242/jcs.111.7.877 · DOI
- 2003, Mol. Biol. Cell., 14, 142, 10.1091/mbc.e02-06-0338 · DOI
- 1998, Cell., 94, 205, 10.1016/S0092-8674(00)81420-8 · DOI
- 2002, Mol. Biol. Cell., 13, 1965, 10.1091/mbc.e01-11-0131 · DOI
- 1999, Mol. Biol. Cell., 10, 3643, 10.1091/mbc.10.11.3643 · DOI
- 2001, Yeast., 18, 1, 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 · DOI
- 2002, Proc. Natl. Acad. Sci. USA., 99, 6767, 10.1073/pnas.092142699 · DOI
- 2001, Science., 292, 1716, 10.1126/science.1060896 · DOI · Paper page
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Cullen, P. J., & Steinberg, F. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0053-7 · Cited by 590
Zavodszky, E., Seaman, M. N. J., Moreau, K., Jimenez-Sanchez, M., Breusegem, S. Y., Harbour, M. E., & Rubinsztein, D. C. (2014) · Nature Communications · doi:10.1038/ncomms4828 · Cited by 466
Model‐guided microarray implicates the retromer complex in Alzheimer's disease
Small, S. A., Kent, K., Pierce, A., Leung, C., Kang, M. S., Okada, H., Honig, L., Vonsattel, J., & Kim, T. (2005) · Annals of Neurology · doi:10.1002/ana.20667 · Cited by 440
Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling
McNally, K. E., Faulkner, R., Steinberg, F., Gallon, M., Ghai, R., Pim, D., Langton, P., Pearson, N., Danson, C. M., Nägele, H., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3610 · Cited by 346
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Metadata
- Authors
- Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R., & Bonifacino, J. S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-04-12
- Volume
- 165
- Issue
- 1
- Pages
- 123-133
- ISSN
- 1540-8140
- 0021-9525
- PMC
- PMC2172094
- Cited by
- 580
- References
- 2
- Language
- en
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