The anterograde transport of the human neuropeptide Y2 receptor is regulated by a subtype specific mechanism mediated by the C-terminus

Walther, Cornelia; Lotze, Jonathan; Beck‐Sickinger, Annette G.; Mörl, Karin

doi:10.1016/j.npep.2012.08.011

Cited by 14 publications

(21 citation statements)

References 58 publications

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“…Thus, it seems reasonable that export motifs or structural determinants might be displayed by the ICL3 instead of the C-terminus. Indeed, deletion of the putative eighth helix of the hY 5 receptor C-terminus had no influence on cell surface expression of the receptor as it has been observed for the hY 1 receptor (Walther et al , 2012 ). Replacing the ICL3 of the hY 5 with the ICL3 of the hY 2 receptor, as well as deletion of large parts of Y5 ICL3 sequences (unpublished results), had no effect on membrane targeting either (Bohme et al , 2008 ).…”

Section: Role Of C-terminal Sequencesmentioning

confidence: 75%

“…Similarly, the motif of the hY 1 receptor 327 F(x) 3 L(x) 3 F 335 resembles the motif of the hY 2 and hY 4 receptors and is also located within the putative eighth helix. Nonetheless, deletion of this motif had no influence on the cell surface targeting of the hY 1 receptor (Walther et al , 2012 ).…”

Section: Role Of C-terminal Sequencesmentioning

confidence: 91%

“…Interestingly, deletion of this motif did not result in impaired ER export but prevented transport of the receptor from the Golgi apparatus to the cell surface (Walther et al , 2012 ). Similarly, the motif of the hY 1 receptor 327 F(x) 3 L(x) 3 F 335 resembles the motif of the hY 2 and hY 4 receptors and is also located within the putative eighth helix.…”

Section: Role Of C-terminal Sequencesmentioning

confidence: 94%

“…Pioneer studies in our laboratory were performed to shed light on the membrane-targeting of human Y receptors. A combination of truncated and point mutants of human Y receptors in HEK293 cells revealed that the molecular mechanisms of all four human Y receptors seem to differ dramatically Walther et al , 2012 ) (Figure 3).…”

Section: The Anterograde Transport Of Y Receptorsmentioning

confidence: 99%

“…With a focus on hY 2 receptor, the sequence motif 332 Y(x) 3 F(x) 3 F 340 located at the very proximal C-terminus was identified to be crucial for ER export (Walther et al , 2012 ). Complete or partial deletion of the motif as well as point mutations from tyrosine/phenylalanine to alanine led to dramatic ER retention of the receptor.…”

Section: Role Of C-terminal Sequencesmentioning

confidence: 99%

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Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors

Babilon

Mörl²,

Beck‐Sickinger³

2013

Biological Chemistry

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Abstract:The neuropeptide Y system is known to be involved in the regulation of many central physiological and pathophysiological processes, such as energy homeostasis, obesity, cancer, mood disorders and epilepsy. Four Y receptor subtypes have been cloned from human tissue (hY 1 , hY 2 , hY 4 and hY 5 ) that form a multiligand/multireceptor system together with their three peptidic agonists (NPY, PYY and PP). Addressing this system for medical application requires on the one hand detailed information about the receptorligand interaction to design subtype-selective compounds. On the other hand comprehensive knowledge about alternative receptor signaling, as well as desensitization, localization and downregulation is crucial to circumvent the development of undesired side-effects and drug resistance. By bringing such knowledge together, highly potent and long-lasting drugs with minimized side-effects can be engineered. Here, current knowledge about Y receptor export, internalization, recycling, and degradation is summarized, with a focus on the human Y receptor subtypes, and is discussed in terms of its impact on therapeutic application.

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Section: Role Of C-terminal Sequencesmentioning

confidence: 75%

Section: Role Of C-terminal Sequencesmentioning

confidence: 91%

Section: Role Of C-terminal Sequencesmentioning

confidence: 94%

Section: The Anterograde Transport Of Y Receptorsmentioning

confidence: 99%

Section: Role Of C-terminal Sequencesmentioning

confidence: 99%

See 3 more Smart Citations

Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors

Babilon

Mörl²,

Beck‐Sickinger³

2013

Biological Chemistry

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Differential barcoding of opioid receptors trafficking

Degrandmaison

Grisé

Parent

et al. 2021

J of Neuroscience Research

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Over the past several years, studies have highlighted the δ-opioid receptor (DOPr) as a promising therapeutic target for chronic pain management. While exhibiting milder undesired effects than most currently prescribed opioids, its specific agonists elicit effective analgesic responses in numerous animal models of chronic pain, including inflammatory, neuropathic, diabetic, and cancer-related pain. However, as compared with the extensively studied μ-opioid receptor, the molecular mechanisms governing its trafficking remain elusive. Recent advances have denoted several significant particularities in the regulation of DOPr intracellular routing, setting it apart from the other members of the opioid receptor family. Although they share high homology, each opioid receptor subtype displays specific amino acid patterns potentially involved in the regulation of its trafficking. These precise motifs or "barcodes" are selectively recognized by regulatory proteins and therefore dictate several aspects of the itinerary of a receptor, including its anterograde transport, internalization, recycling, and degradation. With a specific focus on the regulation of DOPr trafficking, this review will discuss previously reported, as well as potential novel trafficking barcodes within the opioid and nociceptin/orphanin FQ opioid peptide receptors, and their impact in determining distinct interactomes and physiological responses.

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Intracellular Trafficking of Neuropeptide Y Receptors

Mörl

Beck‐Sickinger

2015

Progress in Molecular Biology and Translational Science

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The anterograde transport of the human neuropeptide Y2 receptor is regulated by a subtype specific mechanism mediated by the C-terminus

Cited by 14 publications

References 58 publications

Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors

Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors

Differential barcoding of opioid receptors trafficking

Intracellular Trafficking of Neuropeptide Y Receptors

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