Direct demonstration of discrete Ca2+ microdomains associated with different isoforms of adenylyl cyclase

Willoughby, Debbie; Wachten, Sebastian; Masada, Nanako; Cooper, Dermot M.F.

doi:10.1242/jcs.062067

Cited by 51 publications

(63 citation statements)

References 56 publications

(80 reference statements)

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“…Conversely AC8 hardly detected any fluctuation in Ca 2+ in response to any stimulus other than that triggered by SOCE (Fig. 4) [71]. This observation underlines the different Ca 2+ -dynamics in AC environments, their obviously different composition and it also powerfully supports the observation of the functional responsiveness of AC8 to SOCE and insensitivity to any other Ca 2+ -rise.…”

Section: Measuring Ca 2+ and Camp In Ac Microenvironmentssupporting

confidence: 73%

Store-operated Ca2+-entry and adenylyl cyclase

Cooper

2015

Cell Calcium

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Section: Measuring Ca 2+ and Camp In Ac Microenvironmentssupporting

confidence: 73%

Store-operated Ca2+-entry and adenylyl cyclase

Cooper

2015

Cell Calcium

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“…Some Ca 2+ channels are present in multienzyme protein complexes with proteins that generate their activating ligands (1). It is intriguing to note that Ca 2+ signaling involving the Ca 2+ channel Orai1 that acts in animal immune signaling involves Orai1:adenylyl cyclase protein complexes and microdomains of cyclic nucleotide elevation (40,41). Alternatively, the receptor could act through cytosolic kinase activity to activate channels and initiate downstream CNGC-dependent Ca 2+ signaling cascades.…”

Section: Discussionmentioning

confidence: 99%

Ca ² ⁺ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca ²⁺ channels

Verma

Gehring

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

245

240

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A family of peptide signaling molecules (AtPeps) and their plasma membrane receptor AtPepR1 are known to act in pathogendefense signaling cascades in plants. Little is currently known about the molecular mechanisms that link these signaling peptides and their receptor, a leucine-rich repeat receptor-like kinase, to downstream pathogen-defense responses. We identify some cellular activities of these molecules that provide the context for a model for their action in signaling cascades. AtPeps activate plasma membrane inwardly conducting Ca 2+ permeable channels in mesophyll cells, resulting in cytosolic Ca 2+ elevation. This activity is dependent on their receptor as well as a cyclic nucleotide-gated channel (CNGC2). We also show that the leucine-rich repeat receptor-like kinase receptor AtPepR1 has guanylyl cyclase activity, generating cGMP from GTP, and that cGMP can activate CNGC2-dependent cytosolic Ca 2+ elevation. AtPep-dependent expression of pathogen-defense genes (PDF1.2, MPK3, and WRKY33) is mediated by the Ca 2+ signaling pathway associated with AtPep peptides and their receptor. The work presented here indicates that extracellular AtPeps, which can act as danger-associated molecular patterns, signal by interaction with their receptor, AtPepR1, a plasma membrane protein that can generate cGMP. Downstream from AtPep and AtPepR1 in a signaling cascade, the cGMP-activated channel CNGC2 is involved in AtPep-and AtPepR1-dependent inward Ca 2+ conductance and resulting cytosolic Ca 2+ elevation. The signaling cascade initiated by AtPeps leads to expression of pathogen-defense genes in a Ca 2+ -dependent manner.calcium signaling | plant innate immunity | flagellin receptor 2 | brassinosteroid associated kinase 1

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“…These ACs are regulated by the ubiquitous process of capacitative Ca 2+ entry (CCE) (Parekh and Putney, 2005;Cheng et al, 2011) that is triggered by Ca 2+ store depletion, and are unresponsive to other forms of Ca 2+ rise (Fagan et al, 1996;Martin et al, 2009;Willoughby and Cooper, 2007). The selective regulation of AC8 by CCE depends upon the residence of AC8 in lipid rafts Smith et al, 2002) in close proximity to store-operated Ca 2+ entry channels (Willoughby et al, 2010a). However, little is known about the mechanisms behind the establishment and maintenance of this AC8 'microdomain'.…”

Section: Introductionmentioning

confidence: 99%

Adenylyl cyclase AC8 directly controls its micro-environment by recruiting the actin cytoskeleton in a cholesterol-rich milieu

Ayling

Briddon

Halls

et al. 2012

Journal of Cell Science

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SummaryThe central and pervasive influence of cAMP on cellular functions underscores the value of stringent control of the organization of adenylyl cyclases (ACs) in the plasma membrane. Biochemical data suggest that ACs reside in membrane rafts and could compartmentalize intermediary scaffolding proteins and associated regulatory elements. However, little is known about the organization or regulation of the dynamic behaviour of ACs in a cellular context. The present study examines these issues, using confocal image analysis of various AC8 constructs, combined with fluorescence recovery after photobleaching and fluorescence correlation spectroscopy. These studies reveal that AC8, through its N-terminus, enhances the cortical actin signal at the plasma membrane; an interaction that was confirmed by GST pull-down and immunoprecipitation experiments. AC8 also associates dynamically with lipid rafts; the direct association of AC8 with sterols was confirmed in Förster resonance energy transfer experiments. Disruption of the actin cytoskeleton and lipid rafts indicates that AC8 tracks along the cytoskeleton in a cholesterol-enriched domain, and the cAMP that it produces contributes to sculpting the actin cytoskeleton. Thus, an adenylyl cyclase is shown not just to act as a scaffold, but also to actively orchestrate its own micro-environment, by associating with the cytoskeleton and controlling the association by producing cAMP, to yield a highly organized signalling hub.

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Direct demonstration of discrete Ca2+ microdomains associated with different isoforms of adenylyl cyclase

Abstract: Summary

Cited by 51 publications

References 56 publications

Store-operated Ca2+-entry and adenylyl cyclase

Store-operated Ca2+-entry and adenylyl cyclase

Ca ² ⁺ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca ²⁺ channels

Adenylyl cyclase AC8 directly controls its micro-environment by recruiting the actin cytoskeleton in a cholesterol-rich milieu

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Direct demonstration of discrete Ca2+ microdomains associated with different isoforms of adenylyl cyclase

Abstract: Summary

Cited by 51 publications

References 56 publications

Store-operated Ca2+-entry and adenylyl cyclase

Store-operated Ca2+-entry and adenylyl cyclase

Ca 2 + signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca 2+ channels

Adenylyl cyclase AC8 directly controls its micro-environment by recruiting the actin cytoskeleton in a cholesterol-rich milieu

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Ca ² ⁺ signaling by plant Arabidopsis thaliana Pep peptides depends on AtPepR1, a receptor with guanylyl cyclase activity, and cGMP-activated Ca ²⁺ channels