ArticleMolecular biology of the cell2001
Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Homozygous splice-site variant in ENPP1 underlies generalized arterial calcification of infancy.BMC pediatrics · 2024Article
- ENPP1 deficiency: A clinical update on the relevance of individual variants using a locus-specific patient database.Human mutation · 2022Review
- Diacidic Motifs in the Carboxyl Terminus Are Required for ER Exit and Translocation to the Plasma Membrane of NKCC2.International journal of molecular sciences · 2022Article
- Influenza A Virus M2 Protein Apical Targeting Is Required for Efficient Virus Replication.Journal of virology · 2018Article
- Novel combination of 2-methoxyestradiol and cyclophosphamide enhances the antineoplastic and pro-apoptotic effects on S-180 ascitic tumour cells.Journal of cell communication and signaling · 2018Article
- Casein kinase-mediated phosphorylation of serine 839 is necessary for basolateral localization of the Ca²⁺-activated non-selective cation channel TRPM4.Pflugers Archiv : European journal of physiology · 2015Article
- Basolateral sorting of chloride channel 2 is mediated by interactions between a dileucine motif and the clathrin adaptor AP-1.Molecular biology of the cell · 2015Article
- Mutations in the cytoplasmic domain of the Newcastle disease virus fusion protein confer hyperfusogenic phenotypes modulating viral replication and pathogenicity.Journal of virology · 2013Article
- The apical sorting signal for human GLUT9b resides in the N-terminus.Molecular and cellular biochemistry · 2013Article
- Article
- Multiple evolutionarily conserved Di-leucine like motifs in the carboxyl terminus control the anterograde trafficking of NKCC2.The Journal of biological chemistry · 2012Article
- Cellular function and molecular structure of ecto-nucleotidases.Purinergic signalling · 2012Review
- The role of aspartic acid residues 405 and 416 of the kidney isotype of sodium-bicarbonate cotransporter 1 in its targeting to the plasma membrane.American journal of physiology. Cell physiology · 2012Article
- Tyrosine residues in the cytoplasmic domains affect sorting and fusion activity of the Nipah virus glycoproteins in polarized epithelial cells.Journal of virology · 2010Article
- Putative transmembrane domain 12 of the human organic anion transporter hOAT1 determines transporter stability and maturation efficiency.The Journal of pharmacology and experimental therapeutics · 2010Article
- A highly conserved motif at the COOH terminus dictates endoplasmic reticulum exit and cell surface expression of NKCC2.The Journal of biological chemistry · 2009Article
- Sequence- or position-specific mutations in the carboxyl-terminal FL motif of the kidney sodium bicarbonate cotransporter (NBC1) disrupt its basolateral targeting and alpha-helical structure.The Journal of membrane biology · 2009Article
- Targeting of transmembrane protein shrew-1 to adherens junctions is controlled by cytoplasmic sorting motifs.Molecular biology of the cell · 2006Article
- Physiologic and pathologic functions of the NPP nucleotide pyrophosphatase/phosphodiesterase family focusing on NPP1 in calcification.Purinergic signalling · 2006Article
- A novel cytoplasmic tail MXXXL motif mediates the internalization of prostate-specific membrane antigen.Molecular biology of the cell · 2003Article
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8 authors.
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Abstract
Enzymes of the nucleotide pyrophosphatase/phosphodiesterase (NPPase) family are expressed at opposite surfaces in polarized epithelial cells. We investigated the targeting signal of NPP1, which is exclusively expressed at the basolateral surface. Full-length NPP1 and different constructs and mutants were transfected into the polarized MDCK cell line. Expression of the proteins was analyzed by confocal microscopy and surface biotinylation. The basolateral signal of NPP1 was identified as a di-leucine motif located in the cytoplasmic tail. Mutation of either or both leucines largely redirected NPP1 to the apical surface. Furthermore, addition of the conserved sequence AAASLLAP redirected the apical nucleotide pyrophosphatase/phosphodiesterase NPP3 to the basolateral surface. Full-length NPP1 was not significantly internalized. However, when the cytoplasmic tail was deleted upstream the di-leucine motif or when the six upstream flanking amino acids were deleted, the protein was mainly found intracellularly. Endocytosis experiments indicated that these mutants were endocytosed from the basolateral surface. These results identify the basolateral signal of NPP1 as a short sequence including a di-leucine motif that is dominant over apical determinants and point to the importance of surrounding amino acids in determining whether the signal will function as a basolateral signal only or as an endocytotic signal as well.
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