Organization and Ca2+ Regulation of Adenylyl Cyclases in cAMP Microdomains
TLDR
The regulation of many of the ACs by the ubiquitous second messenger Ca(2+) provides an overarching mechanism for integrating the activities of these two major signaling systems, and cAMP will exhibit distinct kinetics in discrete cellular domains.Abstract:
The adenylyl cyclases are variously regulated by G protein subunits, a number of serine/threonine and tyrosine protein kinases, and Ca2+. In some physiological situations, this regulation can be re...read more
Citations
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Principles of c-di-GMP signalling in bacteria.
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Physiological roles for G protein-regulated adenylyl cyclase isoforms: insights from knockout and overexpression studies.
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TL;DR: The latest on AC knockout and overexpression studies are explored to better understand the roles of G protein regulation of ACs in the brain, olfactory bulb, and heart.
References
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Construction of a full-length ca2+-sensitive adenylyl cyclase/aequorin chimera
Yoshitsugu Nakahashi,Eric J. Nelson,Kent A. Fagan,Elizabeth L. Gonzales,Jean-Louis Guillou,Dermot M.F. Cooper +5 more
TL;DR: This is the first full-length enzyme-aequorin chimera that retains the full biological properties of both aequorin and a Ca2+-sensitive adenylyl cyclase under a variety of physiological conditions.
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Expression of adenylyl cyclase mRNAs in the adult, in developing, and in the Brattleboro rat kidney.
TL;DR: It was demonstrated that AC-6 was the predominant isoform in the adult rat kidney, whereas AC-4, -5, and -9 had a lower expression, and the expression of all these isoforms was decreased in the homozygous Brattleboro rat kidney.
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N-glycosylation and residues Asn805 and Asn890 are involved in the functional properties of type VI adenylyl cyclase.
TL;DR: Glycosylation of ACVI not only affected its catalytic activity in an activator-dependent manner, but also altered its ability to be regulated by a Gαi protein-coupled receptor or by protein kinase C.
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Interactions of the Sulfonylurea Receptor 1 Subunit in the Molecular Assembly of β-Cell KATP Channels
TL;DR: It is concluded that the glibenclamide-binding site includes amino acid residues from both halves of the molecule, that there is strong interaction between different regions of SUR1, that NBD2 is not essential for glibanclamide binding, and that interactions between Kir6.2 and SUR1 participate in ATP-sensitive potassium channel assembly.
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Sensitivity limits for voltage control of P2Y receptor-evoked Ca2+ mobilization in the rat megakaryocyte
TL;DR: It is shown that P2Y receptor‐evoked Ca2+ mobilization is controlled by membrane voltage in a graded and bipolar manner without evidence for a discrete threshold potential.
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