Article (Scientific journals)
Contribution of a tyrosine-based motif to cellular trafficking of wild-type and truncated NPY Y(1) receptors.
Lecat, Sandra; Ouedraogo, Moussa; Cherrier, Thomas et al.
2011In Cellular Signalling, 23 (1), p. 228-38
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Keywords :
Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Clathrin/chemistry/metabolism; HEK293 Cells; Humans; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Neuropeptide Y/pharmacology; RNA Interference; RNA, Small Interfering/metabolism; Receptors, Neuropeptide Y/agonists/genetics/metabolism; Signal Transduction; Transferrin/metabolism; Tyrosine/metabolism; rab5 GTP-Binding Proteins/genetics/metabolism
Abstract :
[en] The human NPY Y(1) receptor undergoes fast agonist-induced internalization via clathrin-coated pits then recycles back to the cell membrane. In an attempt to identify the molecular determinants involved in this process, we studied several C-terminal truncation mutants tagged with EFGP. In the absence of agonist, Y(1) receptors lacking the last 32 C-terminal amino acids (Y(1)Delta32) are constitutively internalized, unlike full-length Y(1) receptors. At steady state, internalized Y(1)Delta32 receptors co-localize with transferrin, a marker of early and recycling endosomes. Inhibition of constitutive internalization of Y(1)Delta32 receptors by hypertonic sucrose or by co-expression of Rab5aS34N, a dominant negative form of the small GTPase Rab5a or depletion of all three isoforms of Rab5 indicates the involvement of clathrin-coated pits. In contrast, a truncated receptor lacking the last 42 C-terminal amino acids (Y(1)Delta42) does not constitutively internalize, consistent with the possibility that there is a molecular determinant responsible for constitutive internalization located in the last 10 amino acids of Y(1)Delta32 receptors. We show that the agonist-independent internalization of Y(1)Delta32 receptors involves a tyrosine-based motif YXXPhi. The potential role of this motif in the behaviour of full-length Y(1) receptors has also been explored. Our results indicate that a C-terminal tyrosine-based motif is critical for the constitutive internalization of truncated Y(1)Delta32 receptors. We suggest that this motif is masked in full-length Y(1) receptors which do not constitutively internalize in the absence of agonist.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Lecat, Sandra
Ouedraogo, Moussa
Cherrier, Thomas ;  Université de Liège - ULiège > GIGA-Research
Noulet, Fanny
Ronde, Philippe
Glasser, Nicole
Galzi, Jean-Luc
Mely, Yves
Takeda, Kenneth
Bucher, Bernard
Language :
English
Title :
Contribution of a tyrosine-based motif to cellular trafficking of wild-type and truncated NPY Y(1) receptors.
Publication date :
2011
Journal title :
Cellular Signalling
ISSN :
0898-6568
eISSN :
1873-3913
Publisher :
Elsevier, Netherlands
Volume :
23
Issue :
1
Pages :
228-38
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Copyright (c) 2010 Elsevier Inc. All rights reserved.
Available on ORBi :
since 26 January 2013

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