Rapid Internalization and Recycling of the Human Neuropeptide Y Y1 Receptor

Gicquiaux, Hervé; Lecat, Sandra; Gaire, Mireille; Dieterlen, Alain; Mély, Yves; Takeda, Kenneth; Bucher, Bernard; Galzi, Jean‐Luc

doi:10.1074/jbc.m107224200

Cited by 111 publications

(123 citation statements)

References 56 publications

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“…It is most likely that this desensitisation is initiated by G-protein receptor kinase (GRK) phosphorylation of the Y 1 receptor and subsequent arrestin binding (Ferguson, 2001). This would be consistent with the promiscuous ability of GRKs and arrestins to regulate many GPCRs (Ferguson, 2001) and the recent demonstration that the Y 1 receptor exhibits agonist-promoted endocytosis (Gicquiaux et al, 2002), a subsequent stage in the GRKFarrestin pathway. GRKs phosphorylate activated receptors specifically; for the well-characterised b 2 -adrenoceptor, this results in a concentration dependence for GRKpromoted events which follows the predicted agonist receptor occupancy (i.e.…”

Section: Discussionsupporting

confidence: 54%

Control of signalling efficacy by palmitoylation of the rat Y₁ receptor

Holliday

Cox

2003

British J Pharmacology

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Section: Discussionsupporting

confidence: 54%

Control of signalling efficacy by palmitoylation of the rat Y₁ receptor

Holliday

Cox

2003

British J Pharmacology

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“…Evidence from our studies pointed that both the constitutive and the PKC-modulated OAT1 internalization occurred partly through a dynamin-and clathrin-dependent pathway. Indeed, treatment of OAT1-expressing cells with ConA, depletion of K ϩ from the cells, or transfection of dominant negative mutants of dynamin-2 into the cells, all of which blocked clathrin-dependent pathway (42)(43)(44)(45), significantly blocked OAT1 internalization (Figs. 8 -10).…”

Section: Discussionmentioning

confidence: 99%

“…To determine whether OAT1 internalizes via clathrin-dependent pathway, the constitutive and PKC-modulated OAT1 internalization were determined under the manipulations that specifically block clathrin-dependent internalization (42)(43)(44)(45): (i) treatment of the cells with concanavalin A (ConA) (Fig. 8a, top panel and Fig.…”

Section: Characterization Of Oat1 In Cos-7mentioning

confidence: 99%

Organic Anion Transporter OAT1 Undergoes Constitutive and Protein Kinase C-regulated Trafficking through a Dynamin- and Clathrin-dependent Pathway

Zhang

Hong

Duan

et al. 2008

Journal of Biological Chemistry

121

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Organic anion transporter 1 (OAT1) mediates the body disposition of a diverse array of environmental toxins and clinically important drugs. Therefore, understanding the regulation of this transporter has profound clinical significance. We previously demonstrate that OAT1 activity was down-regulated by activation of protein kinase C (PKC), kinetically revealed as a decrease in the maximum transport velocity V max without significant change in the substrate affinity K m of the transporter. In the current study, we showed that OAT1 constitutively internalized from and recycled back to the plasma membrane, and PKC activation accelerated OAT1 internalization without affecting OAT1 recycling. We further showed that treatment of OAT1-expressing cells with concanavalin A, depletion of K ؉ from the cells, or transfection of dominant negative mutants of dynamin-2 or Eps15 into the cells, all of which block the clathrindependent endocytotic pathway, significantly blocked constitutive and PKC-regulated OAT1 internalization. We finally showed that OAT1 colocalized with transferrin, a marker for clathrin-dependent endocytosis, at the cell surface and in the EEA1-positive early endosomes. Together, our findings demonstrated for the first time that (i) OAT1 constitutively traffics between plasma membrane and recycling endosomes, (ii) PKC activation down-regulates OAT1 activity by altering already existent OAT1 trafficking, and (iii) OAT1 internalization occurs partly through a dynamin-and clathrin-dependent pathway.

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“…6C). Moreover, as concanavalin A has also been shown to inhibit ligand-induced internalization of plasma membrane receptors (Gicquiaux et al, 2002), we wanted to determine whether ConA-agarose would inhibit the effect of insulin on the BRET signal. Cells were pre-incubated for 20 min in the presence of ConA-agarose and then stimulated for 10 min with 5 nM insulin.…”

Section: Scientific Reportmentioning

confidence: 99%

Dynamics of the interaction between the insulin receptor and protein tyrosine‐phosphatase 1B in living cells

et al. 2003

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scientific report (PTP1B) is a protein-tyrosine phosphatase predominantly localized on intracellular membranes by means of a hydrophobic carboxy-terminal targeting sequence (Frangioni et al., 1992). Evidence for the involvement of PTP1B in insulin action has been provided by studies showing that increased insulin sensitivity is associated with higher levels of tyrosine phosphorylation of the IR and one of its substrates, IR substrate 1 (IRS1), in the liver and skeletal muscle of insulintreated Ptp1B knockout mice (Elchebly et al., 1999). Because PTP1B could be a potential therapeutic target, a better understanding of the interaction between the IR and PTP1B is an important requirement for the development of compounds to improve insulin sensitivity. However, although PTP1B has been shown to interact physically with the IR (Bandyopadhyay et al., 1997), nothing is known about the dynamics of this interaction in living cells.Bioluminescence resonance energy transfer (BRET) allows the study of protein-protein interactions in intact living cells (Angers et al., 2000;Xu et al., 1999). To study the interaction between two proteins, one of them is fused to Renilla luciferase (Rluc) and the other to a yellow fluorescent protein (YFP). The luciferase is excited by a substrate (coelenterazine). If the two proteins are less than 100 Å apart, energy transfer occurs between the luciferase and the YFP, and a signal emitted by the YFP can be detected. We previously showed that this methodology can be used to monitor insulin-induced conformational The dynamics of the interaction of the insulin receptor with a substrate-trapping mutant of protein-tyrosine phosphatase 1B (PTP1B) were monitored in living human embryonic kidney cells using bioluminescence resonance energy transfer (BRET). Insulin dosedependently stimulates this interaction, which could be followed in real time for more than 30 minutes. The effect of insulin on the BRET signal could be detected at early time-points (30 seconds), suggesting that in intact cells the tyrosine-kinase activity of the insulin receptor is tightly controlled by PTP1B. Interestingly, the basal (insulin-independent) interaction of the insulin receptor with PTP1B was much weaker with a soluble form of the tyrosinephosphatase than with the endoplasmic reticulum (ER)-targeted form. Inhibition of insulin-receptor processing using tunicamycin suggests that the basal interaction occurs during insulin-receptor biosynthesis in the ER. Therefore, localization of PTP1B in this compartment might be important for the regulation of insulin receptors during their biosynthesis.

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Rapid Internalization and Recycling of the Human Neuropeptide Y Y1 Receptor

Cited by 111 publications

References 56 publications

Control of signalling efficacy by palmitoylation of the rat Y₁ receptor

Control of signalling efficacy by palmitoylation of the rat Y₁ receptor

Organic Anion Transporter OAT1 Undergoes Constitutive and Protein Kinase C-regulated Trafficking through a Dynamin- and Clathrin-dependent Pathway

Dynamics of the interaction between the insulin receptor and protein tyrosine‐phosphatase 1B in living cells

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Rapid Internalization and Recycling of the Human Neuropeptide Y Y1 Receptor

Cited by 111 publications

References 56 publications

Control of signalling efficacy by palmitoylation of the rat Y1 receptor

Control of signalling efficacy by palmitoylation of the rat Y1 receptor

Organic Anion Transporter OAT1 Undergoes Constitutive and Protein Kinase C-regulated Trafficking through a Dynamin- and Clathrin-dependent Pathway

Dynamics of the interaction between the insulin receptor and protein tyrosine‐phosphatase 1B in living cells

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Control of signalling efficacy by palmitoylation of the rat Y₁ receptor

Control of signalling efficacy by palmitoylation of the rat Y₁ receptor