Seven non-contiguous intracellular residues of the lutropin/choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins (Q22011003)

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English	Seven non-contiguous intracellular residues of the lutropin/choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins	scientific article

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Seven non-contiguous intracellular residues of the lutropin/choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins (English)

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luteinizing hormone/choriogonadotropin receptor

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GOA release 2020-03-11

author name string

K Nakamura

1

author given names

K

author last names

Nakamura

1 reference

PubMed publication ID

7 February 2023

X Liu

2

author given names

X

author last names

Liu

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PubMed publication ID

7 February 2023

M Ascoli

3

author given names

M

author last names

Ascoli

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PubMed publication ID

7 February 2023

language of work or name

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publication date

7 January 2000

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Journal of Biological Chemistry

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275

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1

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241-7

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Mutations that induce constitutive activation and mutations that impair signal transduction modulate the basal and/or agonist-stimulated internalization of the Lutropin/Choriogonadotropin receptor

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The Slow Rate of Internalization of Deglycosylated Human Chorionic Gonadotropin Is Not Due to Its Inability to Stimulate Cyclic Adenosine Monophosphate Accumulation*

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Two mutations of the lutropin/choriogonadotropin receptor that impair signal transduction also interfere with receptor-mediated endocytosis

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Mutation of individual serine residues in the C-terminal tail of the lutropin/choriogonadotropin receptor reveal distinct structural requirements for agonist-induced uncoupling and agonist-induced internalization

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A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands

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Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain

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Characterization of dominant negative arrestins that inhibit beta2-adrenergic receptor internalization by distinct mechanisms

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Linking cargo to vesicle formation: receptor tail interactions with coat proteins.

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The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis

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10.1074/JBC.275.1.241

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