ArticleJournal of cell science2010
Charged residues in the C-terminus of the P2Y1 receptor constitute a basolateral-sorting signal.
Article in Journal of cell science, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Variations of VEGFR2 Chemical Space: Stimulator and Inhibitory Peptides.International journal of molecular sciences · 2024Article
- Loss of P2YJournal of thrombosis and haemostasis : JTH · 2023Article
- A Carboxy-Terminal Monoleucine-Based Motif Participates in the Basolateral Targeting of the Na+/I- Symporter.Endocrinology · 2019Article
- The iodide-transport-defect-causing mutation R124H: a δ-amino group at position 124 is critical for maturation and trafficking of the Na+/I- symporter.Journal of cell science · 2013Article
- Apical targeting of the P2Y(4) receptor is directed by hydrophobic and basic residues in the cytoplasmic tail.American journal of physiology. Cell physiology · 2013Article
- 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
- Polarized sorting and trafficking in epithelial cells.Cell research · 2012Review
- Identification of a novel mono-leucine basolateral sorting motif within the cytoplasmic domain of amphiregulin.Traffic (Copenhagen, Denmark) · 2011Article
- Agonists that increase [Ca²⁺](i) halt the movement of acidic cytoplasmic vesicles in MDCK cells.The Journal of membrane biology · 2011Article
- Pharmacochemistry of the platelet purinergic receptors.Purinergic signalling · 2011Article
- Basolateral sorting signals regulating tissue-specific polarity of heteromeric monocarboxylate transporters in epithelia.Traffic (Copenhagen, Denmark) · 2011Article
- Ser352 and Ser354 in the carboxyl terminus of the human P2Y(1) receptor are required for agonist-promoted phosphorylation and internalization in MDCK cells.British journal of pharmacology · 2011Article
- Coupling of P2Y receptors to G proteins and other signaling pathways.Wiley interdisciplinary reviews. Membrane transport and signalingArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The P2Y(1) receptor is localized to the basolateral membrane of polarized Madin-Darby canine kidney (MDCK) cells. In the present study, we identified a 25-residue region within the C-terminal tail (C-tail) of the P2Y(1) receptor that directs basolateral sorting. Deletion of this sorting signal caused redirection of the receptor to the apical membrane, indicating that the region from the N-terminus to transmembrane domain 7 (TM7) contains an apical-sorting signal that is overridden by a dominant basolateral signal in the C-tail. Location of the signal relative to TM7 is crucial, because increasing its distance from the end of TM7 resulted in loss of basolateral sorting. The basolateral-sorting signal does not use any previously established basolateral-sorting motifs, i.e. tyrosine-containing or di-hydrophobic motifs, for function, and it is functional even when inverted or when its amino acids are scrambled, indicating that the signal is sequence independent. Mutagenesis of different classes of amino acids within the signal identified charged residues (five basic and four acidic amino acids in 25 residues) as crucial determinants for sorting function, with amidated amino acids having a lesser role. Mutational analyses revealed that whereas charge balance (+1 overall) of the signal is unimportant, the total number of charged residues (nine), either positive or negative, is crucial for basolateral targeting. These data define a new class of targeting signal that relies on total charge and might provide a common mechanism for polarized trafficking of epithelial proteins.
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