Guanylyl cyclase expression in specific sensory neurons: A new family of chemosensory receptors

Yu, Sidney; Avery, Leon; Baude, Eric J.; Garbers, David L.

doi:10.1073/pnas.94.7.3384

Cited by 407 publications

(358 citation statements)

References 24 publications

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“…Thus, it has been difficult to make educated guesses regarding the set of chemicals that could be used to systematically examine CR ligand selectivity. Complicating matters, chemosensory neurons in C. elegans also express multiple members of other protein families such as transmembrane guanylyl cyclases, which may also act as chemoreceptors [136,137], further increasing the complexity of the chemosensory receptor repertoire.…”

Section: The Molecules For Taste and Smellmentioning

confidence: 99%

Generation and modulation of chemosensory behaviors in C. elegans

Sengupta

2007

Pflugers Arch - Eur J Physiol

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C. elegans recognizes and discriminates among hundreds of chemical cues using a relatively compact chemosensory nervous system. Chemosensory behaviors are also modulated by prior experience and contextual cues. Because of the facile genetics and genomics possible in this organism, C. elegans provides an excellent system in which to explore the generation of chemosensory behaviors from the level of a single gene to the motor output. This review summarizes the current knowledge on the molecular and neuronal substrates of chemosensory behaviors and chemosensory behavioral plasticity in C. elegans.

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Section: The Molecules For Taste and Smellmentioning

confidence: 99%

Generation and modulation of chemosensory behaviors in C. elegans

Sengupta

2007

Pflugers Arch - Eur J Physiol

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“…In the silkmoth (Bombyx mori), soluble and particulate guanylyl cyclase activity was measured in the antennae, and in Manduca the receptor-like guanylyl cyclase MsGC-I was detected in olfactory receptor neurons (Nighorn et al, 2001). In C. elegans, several different receptor guanylyl cyclases are expressed in olfactory neurons (Yu et al, 1997). Two of these, ODR-1 and DAF-11, are co-expressed in the chemosensory neuron AWC, and mutations to either gene resulted in the abolishment of chemotaxis to all AWC-sensed odorants (Birnby et al, 2001;L'Etoile and Bargmann, 2000).…”

Section: Biochemical Properties Ofmentioning

confidence: 99%

Preliminary characterization of two atypical soluble guanylyl cyclases in the central and peripheral nervous system ofDrosophila melanogaster

Langlais

Stewart

Morton

2004

Journal of Experimental Biology

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SUMMARYConventional soluble guanylyl cyclases form α/β heterodimers that are activated by nitric oxide (NO). Recently, atypical members of the soluble guanylyl cyclase family have been described that include the ratβ2 subunit and MsGC-β3 from Manduca sexta. Predictions from the Drosophila melanogaster genome identify three atypical guanylyl cyclase subunits: Gyc-88E (formerly CG4154), Gyc-89Da (formerly CG14885) and Gyc-89Db (formerly CG14886). Preliminary data showed that transient expression of Gyc-88E in heterologous cells generated enzyme activity in the absence of additional subunits that was slightly stimulated by the NO donor sodium nitroprusside (SNP) but not the NO donor DEA-NONOate or the NO-independent activator YC-1. Gyc-89Db was inactive when expressed alone but when co-expressed with Gyc-88E enhanced the basal and SNP-stimulated activity of Gyc-88E, suggesting that they may form heterodimers in vivo. Here,we describe the localization of Gyc-88E and Gyc-89Db and show that they are expressed in the embryonic and larval central nervous systems and are colocalized in several peripheral neurons that innervate trachea, basiconical sensilla and the sensory cones in the posterior segments of the embryo. We also show that there are two splice variants of Gyc-88E that differ by seven amino acids, although no differences in biochemical properties could be determined. We have also extended our analysis of the NO activation of Gyc-88E and Gyc-89Db, showing that several structurally unrelated NO donors activate Gyc-88E when expressed alone or when co-expressed with Gyc-89Db.

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“…Cell surface guanylyl cyclase receptors are conserved in organisms as varied as worms (Yu et al, 1997), sea urchins (Thorpe and Garbers, 1989), eels (Katafuchi et al, 1994), flies (Liu et al, 1995), rats , and humans . The basic topology of these receptors is maintained in all species.…”

Section: Introductionmentioning

confidence: 99%

A Constitutively “Phosphorylated” Guanylyl Cyclase-linked Atrial Natriuretic Peptide Receptor Mutant Is Resistant to Desensitization

Potter

Hunter

1999

MBoC

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Dephosphorylation of the natriuretic peptide receptor-A (NPR-A) is hypothesized to mediate its desensitization in response to atrial natriuretic peptide (ANP) binding. Recently, we identified six phosphorylation sites within the kinase homology domain of NPR-A and determined that the conversion of these residues to alanine abolished the ability of the receptor to be phosphorylated or to be activated by ANP and ATP. In an attempt to generate a form of NPR-A that mimics a fully phosphorylated receptor but that is resistant to dephosphorylation, we engineered a receptor variant (NPR-A-6E) containing glutamate substitutions at all six phosphorylation sites. Consistent with the known ability of negatively charged glutamate residues to substitute functionally, in some cases, for phosphorylated residues, we found that NPR-A-6E was activated 10-fold by ANP and ATP. As determined by guanylyl cyclase assays, the hormone-stimulated activity of the wild-type receptor declined over time in membrane preparations in vitro, and this loss was blocked by the serine/threonine protein phosphatase inhibitor microcystin. In contrast, the activity of NPR-A-6E was more linear with time and was unaffected by microcystin. The nonhydrolyzable ATP analogue adenosine 5Ј-(␤,␥-imino)-triphosphate was half as effective as ATP in stimulating the wild-type receptor but was equally as potent in stimulating NPR-A-6E, suggesting that ATP is required to keep the wild-type but not 6E variant phosphorylated. Finally, the desensitization of NPR-A-6E in whole cells was markedly blunted compared with that of the wild-type receptor, consistent with its inability to shed the negative charge from its kinase homology domain via dephosphorylation. These data provide the first direct test of the requirement for dephosphorylation in guanylyl cyclase desensitization and they indicate that it is an essential component of this process.

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Guanylyl cyclase expression in specific sensory neurons: A new family of chemosensory receptors

Cited by 407 publications

References 24 publications

Generation and modulation of chemosensory behaviors in C. elegans

Generation and modulation of chemosensory behaviors in C. elegans

Preliminary characterization of two atypical soluble guanylyl cyclases in the central and peripheral nervous system ofDrosophila melanogaster

A Constitutively “Phosphorylated” Guanylyl Cyclase-linked Atrial Natriuretic Peptide Receptor Mutant Is Resistant to Desensitization

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