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Differential Distribution of Low‐Density Lipoprotein‐Receptor‐Related Protein (LRP) and Megalin in Polarized Epithelial Cells is Determined by Their Cytoplasmic Domains

Marzolo, María‐Paz, Yuseff, María Isabel, Retamal, Claudio, Donoso, Maribel, Ezquer, Fernando, Farfán, Pamela, Li, Yonghe, Bu, Guojun·2003·Traffic
DOI 10.1034/j.1600-0854.2003.00081.x
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Abstract

Megalin and the low‐density lipoprotein (LDL) receptor‐related protein (LRP) are two large members of the LDL receptor family that bind and endocytose multiple ligands. The molecular and cellular determinants that dictate the sorting behavior of these receptors in polarized epithelial cells are largely unknown. Megalin is found apically distributed, whereas the limited information on LRP indicates its polarity. We show here that in Madin‐Darby canine kidney cells, both endogenous LRP and a minireceptor containing the fourth ligand‐binding, transmembrane and LRP cytosolic domains were basolaterally sorted. In contrast, minireceptors that either lacked the cytoplasmic domain or had the tyrosine in the NPTY motif mutated to alanine showed a preferential apical distribution. In LLC‐PK1 cells, endogenous megalin was found exclusively in the apical membrane. Studies were also done using chimeric proteins harboring the cytosolic tail of megalin, one with the fourth ligand‐binding domain of LRP and the other two containing the green fluorescent protein as the ectodomain and transmembrane domains of either megalin or LRP. Findings from these experiments showed that the cytosolic domain of megalin is sufficient for apical sorting, and that the megalin transmembrane domain promotes association with lipid rafts. In conclusion, we show that LRP and megalin both contain sorting information in their cytosolic domains that directs opposite polarity, basolateral for LRP and apical for megalin. Additionally, we show that the NPTY motif in LRP is important for basolateral sorting and the megalin transmembrane domain directs association with lipid rafts.

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  • LRP1 has two cytoplasmic tyrosine-based basolateral sorting signals, Y29 and Y63.

    “Low-density lipoprotein receptor–related protein 1 (LRP1) is an endocytic recycling receptor with two cytoplasmic tyrosine-based basolateral sorting signals.”

    From Polarized Traffic of LRP1 Involves AP1B and SNX17 Operating on Y-dependent Sorting Motifs in Different Pathways (2009) · cites this paper as Marzolo et al., 2003

    The Differential Polarized Distribution section reports that mutations at Y29 and Y63 altered LRP localization and concludes that both residues contribute to basolateral sorting. The Discussion says they could be part of basolateral determinants, but does not establish them as two distinct sorting signals; the claim states that more definitively than the paper does. (LLM, conf=0.82)

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  • The differential distribution of LRP and megalin in polarized epithelial cells is determined by their cytoplasmic domains.

    “In a recent study, we reported that the differential distribution of LRP and another large member of the LDL receptor family, megalin, in polarized epithelial cells is determined by their cytoplasmic domains (Marzolo et al, 2003).”

    From Sorting nexin 17 facilitates LRP recycling in the early endosome (2005) · cites this paper as Marzolo et al, 2003

  • The LRP proximal NPTY motif is important for basolateral sorting.

    “Interestingly, it was found that the LRP proximal NPTY motif, identified as the Snx17-binding motif in this study, was important for basolateral sorting; mutation of the tyrosine residue in this motif to alanine resulted in a missorting of LRP to the apical surface.”

    From Sorting nexin 17 facilitates LRP recycling in the early endosome (2005) · cites this paper as Marzolo et al, 2003

  • Mutation of the Y63 residue leads to a nonpolarized distribution of the receptor.

    “The already described mutation of the Y63 residue leads to a nonpolarized distribution of the receptor (Marzolo et al., 2003).”

    From Polarized Traffic of LRP1 Involves AP1B and SNX17 Operating on Y-dependent Sorting Motifs in Different Pathways (2009) · cites this paper as Marzolo et al., 2003

  • LLC-PK1 cells distribute LRP1 in a nonpolarized manner unless exogenous μ1B is expressed by transfection.

    “distributes LRP1 in a nonpolarized manner unless exogenous �1B is expressed by transfection (Marzolo et al., 2003).”

    From Polarized Traffic of LRP1 Involves AP1B and SNX17 Operating on Y-dependent Sorting Motifs in Different Pathways (2009) · cites this paper as Marzolo et al., 2003

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Metadata

Authors
Marzolo, M., Yuseff, M. I., Retamal, C., Donoso, M., Ezquer, F., Farfán, P., Li, Y., & Bu, G.
Venue
Traffic
Publisher
Wiley
Published
2003-04
Volume
4
Issue
4
Pages
273-288
ISSN
  • 1398-9219
  • 1600-0854
DOI
10.1034/j.1600-0854.2003.00081.x
Cited by
79
References
0
Language
en
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 8 d)

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