Increased accuracy of ligand sensing by receptor internalization

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Increased accuracy of ligand sensing by receptor internalization.

Many types of cells can sense external ligand concentrations with cell-surface receptors at extremely high accuracy. Interestingly, ligand-bound receptors are often internalized, a process also known as receptor-mediated endocytosis. While internalization is involved in a vast number of important functions for the life of a cell, it was recently also suggested to increase the accuracy of sensin...

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Increased accuracy of ligand sensing by receptor diffusion on cell surface.

The physical limit with which a cell senses external ligand concentration corresponds to the perfect absorber, where all ligand particles are absorbed and overcounting of same ligand particles does not occur. Here, we analyze how the lateral diffusion of receptors on the cell membrane affects the accuracy of sensing ligand concentration. Specifically, we connect our modeling to neurotransmissio...

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Sensitization of the histamine H1 receptor by increased ligand affinity.

Histamine regulates a variety of physiological processes including inflammation, gastric acid secretion, and neurotransmission. The cellular response to histamine is subject to dynamic control, and exaggerated histamine reactivity in response to cysteinyl leukotrienes and other stimuli is important in a variety of different pathological conditions. The molecular mechanisms controlling histamine...

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Ligand dependency of 5-hydroxytryptamine 2C receptor internalization.

Agonist-induced internalization of G protein-coupled receptors (GPCRs) is a well characterized phenomenon believed to contribute to receptor desensitization. The 5-hydroxytryptamine (5-HT)2C subtype of serotonin receptor is a GPCR that we have shown to internalize upon agonist incubation. In this study, we have examined the effects of 5-HT2C receptor agonists serotonin, Ro 60-0175 [(S)-2-(6-chl...

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Internalization and degradation of natriuretic peptide receptor-A is stimulated by ligand binding

Background Natriuretic peptide receptor-A (NPR-A) is a transmembrane receptor guanylyl cyclase that binds and mediates the effects of atrial and B-type natriuretic peptides (ANP/ BNP). Internalization and ligand-dependent degradation of NPR-A is controversial, in part due to the use of ligand binding studies to predict the cellular location of the receptor. Here, we used a more direct sequentia...

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ژورنال

عنوان ژورنال: Physical Review E

سال: 2010

ISSN: 1539-3755,1550-2376

DOI: 10.1103/physreve.81.021909