Model Systems For The Study Of Seven-Transmembrane-Segment Receptors

Dohlman, H.

doi:10.1146/annurev.biochem.60.1.653

Cited by 197 publications

(221 citation statements)

References 84 publications

(122 reference statements)

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“…At the molecular level, this is characterized by a process known as desensitization, which has been observed in all chemosensory systems, ranging from bacterial chemotaxis to neural transmission in humans, and can vary from complete termination of signaling, as seen in visual and olfactory systems, to graded attenuation of agonist potency in other systems (Dohlman et al, 1991). Desensitization of GPCR-mediated signal transduction is mediated through an impairment of the receptor's ability to activate its corresponding G-protein and is carried out principally through the combined activity of two classes of proteins; G-protein-coupled serine/threonine receptor kinases (GRKs) and arrestins (reviewed in Freedman and Lefkowitz, 1996).…”

Section: Olfactory Mechanismsmentioning

confidence: 99%

Olfactory regulation of mosquito–host interactions

Zwiebel

Takken

2004

Insect Biochemistry and Molecular Biology

274

165

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Mosquitoes that act as disease vectors rely upon olfactory cues to direct several important behaviors that are fundamentally involved in establishing their overall vectorial capacity. Of these, the propensity to select humans for blood feeding is arguably the most important of these olfactory driven behaviors in so far as it significantly contributes to the ability of these mosquitoes to transmit pathogens that cause diseases such as dengue, yellow fever and most significantly human malaria. Here, we review significant advances in behavioral, physiological and molecular investigations into mosquito host preference, with a particular emphasis on studies that have emerged in the post-genomic era that seek to combine these approaches.

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Section: Olfactory Mechanismsmentioning

confidence: 99%

Olfactory regulation of mosquito–host interactions

Zwiebel

Takken

2004

Insect Biochemistry and Molecular Biology

274

165

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“…attenuation of the cellular response upon prolonged or repeated agonist exposure. Extensive studies of β2-adrenergic receptors have revealed the existence of three major mechanisms of receptor desensitization: 1) rapid uncoupling from G-protein, 2) sequestration of receptors into endosomal vesicles, and 3) downregulation of the total number of receptors [87][88][89]. Rapid uncoupling of the ligand-receptor complex from G-protein occurs in a very short time (seconds to minutes after ligand binding) and shifts the receptor to a low-affinity form.…”

Section: Receptor Desensitizationmentioning

confidence: 99%

The angiotensin II type 1 receptor and receptor-associated proteins

et al. 2001

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The mechanisms of regulation, activation and signal transduction of the angiotensin II (Ang II) type 1 (AT1) receptor have been studied extensively in the decade after its cloning. The AT1 receptor is a major component of the renin-angiotensin system (RAS). It mediates the classical biological actions of Ang II. Among the structures required for regulation and activation of the receptor, its carboxyl-terminal region plays crucial roles in receptor internalization, desensitization and phosphorylation. The mechanisms involved in heterotrimeric G-protein coupling to the receptor, activation of the downstream signaling pathway by G proteins and the Ang II signal transduction pathways leading to specific cellular responses are discussed. In addition, recent work on the identification and characterization of novel proteins associated with carboxyl-terminus of the AT1 receptor is presented. These novel proteins will advance our understanding of how the receptor is internalized and recycled as they provide molecular mechanisms for the activation and regulation of G-protein-coupled receptors.

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“…Receptors for N-formylmethionyl peptides (FPR) are among the most thoroughly studied neutrophil receptors and are members of the family of receptors coupled to a guanyl nucleotide-binding protein (G protein). The FPR has recently been cloned (6) and exhibits seven hydrophobic domains, suggesting that this receptor has seven transmembrane segments, analogous to other G protein-coupled receptors (7,8).…”

Section: Lntroductionmentioning

confidence: 99%

Neutrophil chemoattractant receptors and the membrane skeleton

Klotz

Jesaitis

1994

BioEssays

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Signal transduction via receptors for N‐formylmethionyl peptide chemoattractants (FPR) on human neutrophils is a highly regulated process which involves participation of cytoskeletal elements. Evidence exists suggesting that the cytoskeleton and/or the membrane skeleton controls the distribution of FPR in the plane of the plasma membrane, thus controlling the accessibility of FPR to different proteins in functionally distinct domains. In desensitized cells, FPR are restricted to domains which are depleted of G proteins but enriched in cytoskeletal proteins such as actin and fodrin. Thus, the G protein signal transduction partners of FPR become inaccessible to the agonist‐occupied receptor, preventing cell activation. The mechanism of interaction of FPR with the membrane skeleton is poorly understood but evidence is accumulating that suggests a direct binding of FPR (and other receptors) to cytoskeletal proteins such as actin.

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Model Systems For The Study Of Seven-Transmembrane-Segment Receptors

Cited by 197 publications

References 84 publications

Olfactory regulation of mosquito–host interactions

Olfactory regulation of mosquito–host interactions

The angiotensin II type 1 receptor and receptor-associated proteins

Neutrophil chemoattractant receptors and the membrane skeleton

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