scholarly journals Correction: Retraction: Wolfram syndrome 1 and adenylyl cyclase 8 interact at the plasma membrane to regulate insulin production and secretion

2014 ◽  
Vol 17 (1) ◽  
pp. 105-105
Author(s):  
Sonya G. Fonseca ◽  
Fumihiko Urano ◽  
Gordon C. Weir ◽  
Jesper Gromada ◽  
Mark Burcin
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
Wolfram Syndrome ◽  
Insulin Production ◽  
Adenylyl Cyclase 8

scholarly journals Wolfram syndrome 1 and adenylyl cyclase 8 interact at the plasma membrane to regulate insulin production and secretion

2012 ◽  
Vol 14 (10) ◽  
pp. 1105-1112 ◽  
Author(s):  
Sonya G. Fonseca ◽  
Fumihiko Urano ◽  
Gordon C. Weir ◽  
Jesper Gromada ◽  
Mark Burcin
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
Wolfram Syndrome ◽  
Insulin Production ◽  
Adenylyl Cyclase 8

scholarly journals High level expression of transfected G protein αi3subunit is required for plasma membrane targeting and adenylyl cyclase inhibition in NIH 3T3 fibroblasts

FEBS Letters ◽  
1992 ◽  
Vol 312 (2-3) ◽  
pp. 223-228 ◽  
Author(s):  
Sylvie Hermouet ◽  
Philippe de Mazancourt ◽  
Allen M. Spiegel ◽  
Marilyn Gist Farquhar ◽  
Bridget S. Wilson
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
G Protein ◽  
Membrane Targeting ◽  
High Level Expression ◽  
3T3 Fibroblasts ◽  
High Level ◽  
Nih 3T3

scholarly journals Identification of FDA-Approved Small Molecules Capable of Disrupting the Calmodulin–Adenylyl Cyclase 8 Interaction through Direct Binding to Calmodulin

2017 ◽  
Vol 9 (2) ◽  
pp. 346-357 ◽  
Author(s):  
Michael P. Hayes ◽  
Monica Soto-Velasquez ◽  
C. Andrew Fowler ◽  
Val J. Watts ◽  
David L. Roman
Keyword(s):  
Small Molecules ◽  
Adenylyl Cyclase ◽  
Direct Binding ◽  
Adenylyl Cyclase 8

scholarly journals Calcium influx activates adenylyl cyclase 8 for sustained insulin secretion in rat pancreatic beta cells

Diabetologia ◽  
2014 ◽  
Vol 58 (2) ◽  
pp. 324-333 ◽  
Author(s):  
Haiqiang Dou ◽  
Changhe Wang ◽  
Xi Wu ◽  
Lijun Yao ◽  
Xiaoyu Zhang ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Adenylyl Cyclase ◽  
Beta Cells ◽  
Pancreatic Beta Cells ◽  
Calcium Influx ◽  
Adenylyl Cyclase 8

Dopamine recruits D1A receptors to Na-K-ATPase-rich caveolar plasma membranes in rat renal proximal tubules

2004 ◽  
Vol 287 (5) ◽  
pp. F921-F931 ◽  
Author(s):  
Meghna Trivedi ◽  
Vihang A. Narkar ◽  
Tahir Hussain ◽  
Mustafa F. Lokhandwala
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
Plasma Membranes ◽  
Radioligand Binding ◽  
Sch 23390 ◽  
Sucrose Density Gradient ◽  
Proximal Tubules ◽  
Sodium Reabsorption ◽  
Sprague Dawley ◽  
Renal Proximal Tubules

Activation of dopamine D1A receptors in renal proximal tubules causes inhibition of sodium transporters (Na-K-ATPase and Na/H exchanger), leading to a decrease in sodium reabsorption. In addition to being localized on the plasma membrane, D1A receptors are mainly present in intracellular compartments under basal conditions. We observed, using [3H]SCH-23390 binding and immunoblotting, that dopamine recruits D1A receptors to the plasma membrane in rat renal proximal tubules. Furthermore, radioligand binding and/or immunoblotting experiments using pharmacological modulators showed that dopamine-induced D1A receptor recruitment requires activation of cell surface D1-like receptors, activation of adenylyl cyclase, and intact endocytic vesicles with internal acidic pH. A key finding of this study was that these recruited D1A receptors were functional because they potentiated dopamine-induced [35S]GTPγS binding, cAMP accumulation, and Na-K-ATPase inhibition. Interestingly, dopamine increased immunoreactivity of D1A receptors specifically in caveolin-rich plasma membranes isolated by a sucrose density gradient. In support of this observation, coimmunoprecipitation studies showed that D1A receptors interacted with caveolin-2 in an agonist-dependent fashion. The caveolin-rich plasma membranes had a high content of the α1-subunit of Na-K-ATPase, which is a downstream target of D1A receptor signaling in proximal tubules. These results show that dopamine, via the D1-like receptor-adenylyl cyclase pathway, recruits D1A receptors to the plasma membrane. These newly recruited receptors couple to G proteins, increase cAMP, and participate in dopamine-mediated inhibition of Na-K-ATPase in proximal tubules. Moreover, dopamine-induced recruitment of D1A receptors to the caveolin-rich plasma membranes brings them in close proximity to targets such as Na-K-ATPase in proximal tubules of Sprague-Dawley rats.

Implication of adenylyl cyclase 8 in pathological smooth muscle cell migration occurring in rat and human vascular remodelling

2010 ◽  
Vol 221 (3) ◽  
pp. 331-342 ◽  
Author(s):  
Marie Gueguen ◽  
Zela Keuylian ◽  
Véronique Mateo ◽  
Nathalie Mougenot ◽  
Anne-Marie Lompré ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Cell Migration ◽  
Smooth Muscle Cell ◽  
Adenylyl Cyclase ◽  
Muscle Cell ◽  
Vascular Remodelling ◽  
Smooth Muscle Cell Migration ◽  
Adenylyl Cyclase 8

scholarly journals G protein-regulated endocytic trafficking of adenylyl cyclase type 9

2020 ◽  
Author(s):  
André M. Lazar ◽  
Roshanak Irannejad ◽  
Tanya A. Baldwin ◽  
Aparna A. Sundaram ◽  
J. Silvio Gutkind ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Adenylyl Cyclase ◽  
G Protein ◽  
Subcellular Location ◽  
Endocytic Pathway ◽  
Heterotrimeric G Proteins ◽  
Camp Production ◽  
Stimulation Of

SummaryGPCRs are increasingly recognized to initiate signaling via heterotrimeric G proteins as they move through the endocytic network, but little is known about how relevant G protein effectors are localized. Here we report dynamic trafficking of adenylyl cyclase type 9 (AC9) from the plasma membrane to endosomes, while adenylyl cyclase type 1 (AC1) remains in the plasma membrane, and stimulation of AC9 trafficking by ligand-induced activation of Gs-coupled GPCRs or Gs. AC9 transits a similar dynamin-dependent early endocytic pathway as activated GPCRs but, in contrast to GPCR trafficking which is regulated by β-arrestin but not Gs, AC9 trafficking is regulated by Gs but not β-arrestin. We also show that AC9, but not AC1, contributes to cAMP production from endosomes. These results reveal dynamic and isoform-specific trafficking of adenylyl cyclase in the endocytic network, and a discrete role of a heterotrimeric G protein in controlling subcellular location of a relevant effector.

scholarly journals Retargeting from the CR3 to the LFA-1 receptor uncovers the adenylyl cyclase enzyme–translocating segment of Bordetella adenylate cyclase toxin

2020 ◽  
Vol 295 (28) ◽  
pp. 9349-9365
Author(s):  
Jiri Masin ◽  
Adriana Osickova ◽  
David Jurnecka ◽  
Nela Klimova ◽  
Humaira Khaliq ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Adenylyl Cyclase ◽  
Specific Capacity ◽  
Target Cells ◽  
Jurkat T Cells ◽  
Membrane Interaction ◽  
The Family ◽  
Adenylate Cyclase Toxin ◽  
Complement Receptor 3

The Bordetella adenylate cyclase toxin-hemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the αLβ2 integrin LFA-1 (CD11a/CD18) of leukocytes and can promiscuously bind and also permeabilize many other cells. CyaA bears an N-terminal adenylyl cyclase (AC) domain linked to a pore-forming RTX cytolysin (Hly) moiety, binds the complement receptor 3 (CR3, αMβ2, CD11b/CD18, or Mac-1) of myeloid phagocytes, penetrates their plasma membrane, and delivers the AC enzyme into the cytosol. We constructed a set of CyaA/HlyA chimeras and show that the CyaC-acylated segment and the CR3-binding RTX domain of CyaA can be functionally replaced by the HlyC-acylated segment and the much shorter RTX domain of HlyA. Instead of binding CR3, a CyaA1-710/HlyA411-1024 chimera bound the LFA-1 receptor and effectively delivered AC into Jurkat T cells. At high chimera concentrations (25 nm), the interaction with LFA-1 was not required for CyaA1-710/HlyA411-1024 binding to CHO cells. However, interaction with the LFA-1 receptor strongly enhanced the specific capacity of the bound CyaA1-710/HlyA411-1024 chimera to penetrate cells and deliver the AC enzyme into their cytosol. Hence, interaction of the acylated segment and/or the RTX domain of HlyA with LFA-1 promoted a productive membrane interaction of the chimera. These results help delimit residues 400–710 of CyaA as an “AC translocon” sufficient for translocation of the AC polypeptide across the plasma membrane of target cells.

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