9 Adenylyl cyclases and alcohol

1997 ◽  
pp. 173-193 ◽  
Author(s):  
Boris Tabakoff ◽  
Paula L. Hoffman
Keyword(s):  
Adenylyl Cyclases

Elucidating cyclic AMP signaling in subcellular domains with optogenetic tools and fluorescent biosensors

2019 ◽  
Vol 47 (6) ◽  
pp. 1733-1747 ◽  
Author(s):  
Christina Klausen ◽  
Fabian Kaiser ◽  
Birthe Stüven ◽  
Jan N. Hansen ◽  
Dagmar Wachten
Keyword(s):  
Cyclic Amp ◽  
Adenosine Monophosphate ◽  
Adenylyl Cyclases ◽  
Temporal Precision ◽  
Fluorescent Biosensors ◽  
Subcellular Domains ◽  
Spatio Temporal ◽  
Hydrolysis Of ◽  
Shed Light ◽  
Cyclic Amp Signaling

The second messenger 3′,5′-cyclic nucleoside adenosine monophosphate (cAMP) plays a key role in signal transduction across prokaryotes and eukaryotes. Cyclic AMP signaling is compartmentalized into microdomains to fulfil specific functions. To define the function of cAMP within these microdomains, signaling needs to be analyzed with spatio-temporal precision. To this end, optogenetic approaches and genetically encoded fluorescent biosensors are particularly well suited. Synthesis and hydrolysis of cAMP can be directly manipulated by photoactivated adenylyl cyclases (PACs) and light-regulated phosphodiesterases (PDEs), respectively. In addition, many biosensors have been designed to spatially and temporarily resolve cAMP dynamics in the cell. This review provides an overview about optogenetic tools and biosensors to shed light on the subcellular organization of cAMP signaling.

scholarly journals Functional Characterization of the Adenylyl Cyclase Genesgs-1by Analysis of a Mutational Spectrum inCaenorhabditis elegans

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 133-142 ◽  
Author(s):  
Celine Moorman ◽  
Ronald H A Plasterk
Keyword(s):  
Life Span ◽  
Adenylyl Cyclase ◽  
Neuronal Degeneration ◽  
Functional Characterization ◽  
Adenylyl Cyclases ◽  
Loss Of Function ◽  
C Elegans ◽  
Larval Stages ◽  
Pharyngeal Pumping

AbstractThe sgs-1 (suppressor of activated Gαs) gene encodes one of the four adenylyl cyclases in the nematode C. elegans and is most similar to mammalian adenylyl cyclase type IX. We isolated a complete loss-of-function mutation in sgs-1 and found it to result in animals with retarded development that arrest in variable larval stages. sgs-1 mutant animals exhibit lethargic movement and pharyngeal pumping and (while not reaching adulthood) have a mean life span that is >50% extended compared to wild type. An extensive set of reduction-of-function mutations in sgs-1 was isolated in a screen for suppressors of a neuronal degeneration phenotype induced by the expression of a constitutively active version of the heterotrimeric Gαs subunit of C. elegans. Although most of these mutations change conserved residues within the catalytic domains of sgs-1, mutations in the less-conserved transmembrane domains are also found. The sgs-1 reduction-of-function mutants are viable and have reduced locomotion rates, but do not show defects in pharyngeal pumping or life span.

scholarly journals Studies on Receptor-mediated Activation of Adenylyl Cyclases

1974 ◽  
Vol 249 (24) ◽  
pp. 7867-7873 ◽  
Author(s):  
Lutz Birnbaumer ◽  
Po-Chang Yang
Keyword(s):  
Adenylyl Cyclases

scholarly journals Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases.

1994 ◽  
Vol 269 (8) ◽  
pp. 6093-6100 ◽  
Author(s):  
R. Taussig ◽  
W.J. Tang ◽  
J.R. Hepler ◽  
A.G. Gilman
Keyword(s):  
Adenylyl Cyclases ◽  
Bidirectional Regulation

scholarly journals Studies on Receptor-mediated Activation of Adenylyl Cyclases

1974 ◽  
Vol 249 (24) ◽  
pp. 7886-7891 ◽  
Author(s):  
Tatsuo Nakahara ◽  
Lutz Birnbaumer
Keyword(s):  
Adenylyl Cyclases

A nuclear location for Ca2+-activated adenylyl cyclases I and III in neurones

2001 ◽  
Vol 91 (1-2) ◽  
pp. 43-49 ◽  
Author(s):  
Nicola A. Parkinson ◽  
Stephen R. Bolsover
Keyword(s):  
Adenylyl Cyclases ◽  
Nuclear Location

scholarly journals Signaling through Adenylyl Cyclase Is Essential for Hyphal Growth and Virulence in the Pathogenic FungusCandida albicans

2001 ◽  
Vol 12 (11) ◽  
pp. 3631-3643 ◽  
Author(s):  
Cintia R. C. Rocha ◽  
Klaus Schröppel ◽  
Doreen Harcus ◽  
Anne Marcil ◽  
Daniel Dignard ◽  
...  
Keyword(s):  
Mouse Model ◽  
Adenylyl Cyclase ◽  
Sequence Similarity ◽  
Hyphal Growth ◽  
Antifungal Drugs ◽  
Growth Defect ◽  
Adenylyl Cyclases ◽  
Gene Encoding ◽  
Mutant Cells

The human fungal pathogen Candida albicans switches from a budding yeast form to a polarized hyphal form in response to various external signals. This morphogenetic switching has been implicated in the development of pathogenicity. We have cloned theCaCDC35 gene encoding C. albicansadenylyl cyclase by functional complementation of the conditional growth defect of Saccharomyces cerevisiae cells with mutations in Ras1p and Ras2p. It has previously been shown that these Ras homologues regulate adenylyl cyclase in yeast. The C. albicans adenylyl cyclase is highly homologous to other fungal adenylyl cyclases but has less sequence similarity with the mammalian enzymes. C. albicans cells deleted for both alleles ofCaCDC35 had no detectable cAMP levels, suggesting that this gene encodes the only adenylyl cyclase in C. albicans. The homozygous mutant cells were viable but grew more slowly than wild-type cells and were unable to switch from the yeast to the hyphal form under all environmental conditions that we analyzed in vitro. Moreover, this morphogenetic switch was completely blocked in mutant cells undergoing phagocytosis by macrophages. However, morphogenetic switching was restored by exogenous cAMP. On the basis of epistasis experiments, we propose that CaCdc35p acts downstream of the Ras homologue CaRas1p. These epistasis experiments also suggest that the putative transcription factor Efg1p and components of the hyphal-inducing MAP kinase pathway depend on the function of CaCdc35p in their ability to induce morphogenetic switching. Homozygouscacdc35Δ cells were unable to establish vaginal infection in a mucosal membrane mouse model and were avirulent in a mouse model for systemic infections. These findings suggest that fungal adenylyl cyclases and other regulators of the cAMP signaling pathway may be useful targets for antifungal drugs.

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