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Lipoprotein receptors: new roles for ancient proteins

Willnow, Thomas E., Nykjaer, Anders, Herz, Joachim·1999·Nature Cell Biology
DOI 10.1038/14109
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Abstract

Lipoprotein receptors used to be viewed simply as the means by which cells were supplied with lipids for energy production and membrane synthesis. This perception has now changed dramatically. Megalin, a member of the low density lipoprotein receptor gene family, turns out to mediate the endocytic uptake of retinoids and steroids, thus helping to regulate their biological function. Other members of this receptor family interact with cytosolic signalling proteins, giving this evolutionarily ancient family of receptors an entirely unexpected new role as transducers of extracellular signals.

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  • LDL receptor family members contain NPXY motif(s) specifically recognized by Dab2.

    “The members of the LDL (low density lipoprotein) receptor family contain the NPXY motif(s) specifically recognized by Dab2”

    From Endocytosis and Physiology: Insights from Disabled-2 Deficient Mice (2016) · cites this paper as Willnow et al., 1999

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Research works printed but not linked: 68

  1. Goldstein, J. L. & Brown, M. S. in The Metabolic Basis of Inherited Disease Vol. 6 (eds Scriver, C.R., Beaudet, A.L., Sly, W. S. & Valle, D.) 1215–1250 (McGraw-Hill, New York, 1989).
  2. Hobbs, H. H., Russell, D. W., Brown, M. S. & Goldstein, J. L. The LDL receptor locus and familial hypercholesterolemia: Mutational analysis of a membrane protein. Annu. Rev. Genet. 24, 133–170 (1990). · DOI · Paper page
  3. 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. 265, 3116– 3123 (1990). · DOI · Paper page
  4. Esser, V., Limbird, L. E., Brown, M. S., Goldstein, J. L. & Russell, D. W. Mutational analysis of the ligand binding domain of the low density lipoprotein receptor. J. Biol. Chem. 263, 13282–13290 ( 1988). · DOI · Paper page
  5. Fass, D., Blacklow, S., Kim, P. S. & Berger, J. M. Molecular basis of familial hypercholesterolaemia from structure of the LDL receptor module . Nature 388, 691–693 (1997). · DOI
  6. Bansal, A. & Gierasch, L. M. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell 67, 1195–1201 (1991). · DOI · Paper page
  7. Südhof, T. C., Goldstein, J. L., Brown, M. S. & Russell, D. W. The LDL receptor gene: A mosaic of exons shared with different proteins. Science 228, 815–822 ( 1985). · DOI · Paper page
  8. Gilbert, W. DNA sequencing and gene structure. Science 214, 1305–1312 (1981). · DOI
  9. Herz, J. et al. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J. 7, 4119–4127 (1988). · DOI
  10. Saito, A., Pietromonaco, S., Loo, A. K.-C. & Farquhar, M. G. Complete cloning and sequencing of rat gp330/‘‘megalin’’. A distinctive member of the low density lipoprotein receptor gene family. Proc. Natl Acad. Sci. USA 91, 9725– 9729 (1994). · DOI
  11. Takahashi, S., Kawarabayasi, Y., Nakai, T., Sakai, J. & Yamamoto, T. Rabbit very low density lipoprotein receptor: A low density lipoprotein receptor-like protein with distinct ligand specificity. Proc. Natl Acad. Sci. USA 89, 9252–9256 (1992). · DOI
  12. Kim, D.-H. et al. Human apolipoprotein E receptor 2. J. Biol. Chem. 271, 8373–8380 ( 1996). · DOI · Paper page
  13. Novak, S., Hiesberger, T., Schneider, W. J. & Nimpf, J. A new low density lipoprotein receptor homologue with 8 ligand binding repeats in brain of chicken and mouse. J. Biol. Chem. 271, 11732–11736 (1996). · DOI · Paper page
  14. Krieger, M. & Herz, J. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu. Rev. Biochem. 63, 601 –637 (1994). · DOI
  15. Gliemann, J. Receptors of the low density lipoprotein receptor family in man. Multiple functions of the large family members via interaction with complex ligands . Biol. Chem. 379, 951– 964 (1998).
  16. Yochem, J. & Greenwald, I. A gene for a low density lipoprotein receptor-related protein in the nematode Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 90, 4572– 4576 (1993). · DOI
  17. Trommsdorff, M., Borg, J. P., Margolis, B. & Herz, J. Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein. J. Biol. Chem. 273, 33556–33560 (1998). · DOI · Paper page
  18. Kita, T. et al. Hepatic uptake of chylomicron remnants in WHHL rabbits: A mechanism genetically distinct from the low density lipoprotein receptor. Proc. Natl Acad. Sci. USA 79, 3623– 3627 (1982). · DOI · Paper page
  19. Willnow, T. E., Sheng, Z., Ishibashi, S. & Herz, J. Inhibition of hepatic chylomicron remnant uptake by gene transfer of a receptor antagonist. Science 264, 1471–1474 ( 1994). · DOI
  20. Strickland, D. K. et al. Sequence identity between the a2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor. J. Biol. Chem. 265, 17401–17404 (1990). · DOI · Paper page
  21. Kristensen, T. et al. Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the a2-macroglobulin receptor. FEBS Lett. 276, 151–155 ( 1990). · DOI
  22. Ishibashi, S. et al. Hypercholesterolemia in LDL receptor knockout mice and its reversal by adenovirus-mediated gene delivery. J. Clin. Invest. 92, 883–893 ( 1993). · DOI · Paper page
  23. Herz, J., Clouthier, D. E. & Hammer, R. E. LDL receptor-related protein internalizes and degrades uPA/PAI-1 complexes and is essential for embryo implantation. Cell 71, 411–421 ( 1992). · DOI · Paper page
  24. Rajewsky, K. et al. Conditional gene targeting. J. Clin. Invest. 98, 600–603 (1996). · DOI
  25. Rohlmann, A., Gotthardt, M., Willnow, T. E., Hammer, R. E. & Herz, J. Sustained somatic gene inactivation by viral transfer of Cre recombinase. Nature Biotechnol. 14, 1562–1565 (1996). · DOI
  26. Christensen, E. I., Birn, H., Verroust, P. & Moestrup, S. K. Membrane receptors for endocytosis in the renal proximal tubules. Int. Rev. Cytol. 180, 237–284 ( 1998). · DOI
  27. Orlando, R. A. et al. Megalin is an endocytic receptor for insulin. J. Am. Soc. Nephrol. 9, 1759–1766 (1998). · DOI
  28. Nykjaer, A. et al. An endocytic pathway essential for renal uptake and activation of the steroid 25-(OH) vitamin D3. Cell 96, 507–515 (1999). · DOI
  29. Haddad, J. G. Plasma vitamin D-binding protein (Gc-globulin): Multiple tasks. J. Steroid Biochem. 53, 1–6 (1995). · DOI
  30. Newcomer, M. E., Jamison, R. S. & Ong, D. E. Structure and function of retinoid-binding proteins . Subcell. Biochem. 30, 53– 80 (1998). · DOI
  31. Christensen, E. I. et al. Evidence for an essential role of megalin in transepithelial transport of retinol. J. Am. Soc. Nephrol. 10, 685–695 (1999). · DOI
  32. Safadi, F. F. et al. Osteopathy and resistance to vitamin D toxicity in mice null for vitamin D binding protein. J. Clin. Invest. 103 , 239–251 (1999). · DOI
  33. Leheste, J.-R. et al. Megalin knockout mice as an animal model of low molecular weight proteinuria. Am. J. Pathol. (in the press). · DOI
  34. Rosner, W. Plasma steroid-binding proteins. Endocrinol. Metab. Clin. North Am. 20, 697–720 ( 1991). · DOI
  35. Maden, M. Vertebrate development: a nervous vitamin. Curr. Biol. 8, R846–R849 (1998). · DOI
  36. Mendel, C. M. The free hormone hypothesis: a physiologically based mathematical model. Endocr. Rev. 10, 232–274 (1989). · DOI · Paper page
  37. Bikle, D. D. et al. Assessment of the free fraction of 25-hydroxyvitamin D in serum and its regulation by albumin and the vitamin D-binding protein. J. Clin. Endocrinol. Metab. 63, 954– 959 (1986). · DOI
  38. Bikle, D. D., Siiteri, P. K., Ryzen, E. & Haddad, J. G. Serum protein binding of 1,25-dihydroxyvitamin D: a reevaluation by direct measurement of free metabolite levels. J. Clin. Endocr. Metab. 61, 969–975 ( 1985). · DOI
  39. Gerard, A. et al. Electron microscope radioautographic evidence of in vivo androgen-binding protein internalization in the rat epididymis principal cells. Endocrinology 122, 1297–1307 (1988). · DOI
  40. Joseph, D. R. Sequence and functional relationships between androgen-binding protein/sex hormone-binding globulin and its homologs protein S, Gas6, laminin, and agrin . Steroids. 62, 578–588 (1997). · DOI
  41. Porto, C. S., Gunsalus, G. L., Bardin, C. W., Phillips, D. M. & Musto, N. A. Receptor-mediated endocytosis of an extracellular steroid-binding protein (TeBG) in MCF-7 human breast cancer cells. Endocrinology 129, 436–445 (1991). · DOI
  42. Bavik, C., Ward, S. J. & Chambon, P. Developmental abnormalities in cultured mouse embryos deprived of retinoic acid by inhibition of yolk-sac retinol binding protein synthesis. Proc. Natl Acad. Sci. USA 93, 3110–3114 (1996). · DOI
  43. Ward, S. J., Chambon, P., Ong, D. E. & Bavik, C. A retinol-binding protein receptor-mediated mechanism for uptake of vitamin A to postimplantation rat embryos. Biol. Reprod. 57, 751– 755 (1997). · DOI
  44. Morriss-Kay, G. M. & Ward, S. J. Retinoids and mammalian development. Int. Rev. Cytol. 188, 73–131 (1999). · DOI
  45. Senoo, H. et al. Internalization of retinol-binding protein in parenchymal and stellate cells of rat liver. J. Lipid. Res. 31, 1229–1239 (1990). · DOI
  46. Matarese, V. & Lodish, H. F. Specific uptake of retinol-binding protein by variant F9 cell lines. J. Biol. Chem. 268 , 18859–18865 (1993). · DOI
  47. Tosetti, F., Campelli, F. & Levi, G. Studies on the cellular uptake of retinol binding protein and retinol. Exp. Cell Res. 250, 423– 433 (1999). · DOI
  48. Kang, D. E. et al. Genetic association of the low-density lipoprotein receptor-related protein gene (LRP), an apolipoprotein E receptor, with late-onset Alzheimer"s disease. Neurology 49, 56– 61 (1997). · DOI · Paper page
  49. Schmechel, D. E. et al. Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer"s disease . Proc. Natl Acad. Sci. USA 90, 9649– 9653 (1993). · DOI · Paper page
  50. Chartier-Harlin, M. C. et al. Early-onset Alzheimer"s disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene. Nature 353, 844–846 (1991). · DOI · Paper page
  51. Kounnas, M. Z. et al. LDL receptor-related protein, a multifunctional apoE receptor, binds secreted β-amyloid precursor protein and mediates its degradation . Cell 82, 331–340 (1995). · DOI · Paper page
  52. Riddell, D. R., Graham, A. & Owen, J. S. Apolipoprotein E inhibits platelet aggregation through the L-arginine:nitric oxide pathway. Implications for vascular disease. J. Biol. Chem. 272, 89–95 (1997). · DOI · Paper page
  53. Howell, B. W., Lanier, L. M., Frank, R., Gertler, F. B. & Cooper, J. A. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids . Mol. Cell Biol. 19, 5179– 5188 (1999). · DOI · Paper page
  54. Blaikie, P. et al. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269, 32031–32034 (1994). · DOI
  55. Pawson, T. & Scott, J. D. Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075– 2080 (1997). · DOI · Paper page
  56. Borg, J. P., Ooi, J., Levy, E. & Margolis, B. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16, 6229–6241 (1996). · DOI · Paper page
  57. Zambrano, N. et al. Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer’s beta- amyloid precursor proteins. J. Biol. Chem. 272 , 6399–6405 (1997). · DOI
  58. Trommsdorff, M. et al. Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. Cell 97, 689–701 (1999). · DOI · Paper page
  59. Howell, B. W., Hawkes, R., Soriano, P. & Cooper, J. A. Neuronal position in the developing brain is regulated by mouse disabled-1. Nature 389, 733–737 ( 1997). · DOI · Paper page
  60. Ware, M. L. et al. Aberrant splicing of a mouse disabled homolog, mdab1, in the scrambler mouse. Neuron 19, 239– 249 (1997). · DOI
  61. Howell, B. W., Herrick, T. M. & Cooper, J. A. Reelin-induced tryosine phosphorylation of disabled 1 during neuronal positioning. Genes Dev. 13, 643–648 (1999). · DOI · Paper page
  62. Howell, B. W., Gertler, F. B. & Cooper, J. A. Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. EMBO J. 16, 121 –132 (1997). · DOI · Paper page
  63. Koleske, A. J. et al. Essential roles for the Abl and Arg tyrosine kinases in neurulation . Neuron 21, 1259–1272 (1998). · DOI
  64. Hsu, H. Y., Hajjar, D. P., Khan, K. M. & Falcone, D. J. Ligand binding to macrophage scavenger receptor-A induces urokinase-type plasminogen activator expression by a protein kinase-dependent signaling pathway. J. Biol. Chem. 273, 1240–1246 (1998). · DOI
  65. Hiltunen, T.P. & Yla-Herttuala, S. Expression of lipoprotein receptors in atherosclerotic lesions. Atherosclerosis 137 (Suppl.), 81–88 ( 1998). · DOI
  66. Porto, C. S. et al. Receptors for androgen-binding proteins: internalization and intracellular signalling. J. Steroid Biochem. Mol. Biol. 53, 561–565 (1995). · DOI
  67. Rosner, W., Hryb, D.J., Khan, M.S., Nakhla, A. M. & Romas, N.A. Sex hormone-binding globulin mediates steroid hormone signal transduction at the plasma membrane. J. Steroid Biochem. Mol. Biol. 69, 481–485 ( 1999). · DOI
  68. Goretzki, L. & Mueller, B.M. Low-density-lipoprotein-receptor-related protein (LRP) interacts with a GTP-binding protein. Biochem. J. 336, 381–386 ( 1998). · DOI · Paper page

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Metadata

Authors
Willnow, T. E., Nykjaer, A., & Herz, J.
Venue
Nature Cell Biology
Publisher
Springer Science and Business Media LLC
Published
1999-10
Volume
1
Issue
6
Pages
E157-E162
ISSN
  • 1465-7392
  • 1476-4679
DOI
10.1038/14109
Cited by
181
References
6
Language
en
Licence
www.springer.com/tdm (tdm)

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