Calcium-modulated ciliary membrane guanylate cyclase transduction machinery: Constitution and operational principles

Duda, Teresa; Fik-Rymarkiewicz, Ewa; Venkataraman, V.; Krishnan, Anuradha; Sharma, Rameshwar K.

doi:10.1007/s11010-005-4955-2

Cited by 14 publications

(21 citation statements)

References 43 publications

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“…The samples contained saturating amount of Ca 2+ and increasing concentrations of neurocalcin δ; the control samples contained no Ca 2+ . In accordance with the earlier results and conclusions [14, 15, 24], neurocalcin δ-modulated Ca 2+ signaling of ONE-GC was strictly Ca 2+ -dependent (Fig. 2B).…”

Section: Resultssupporting

confidence: 93%

“…These results also show that among membrane guanylate cyclases ONE-GC transduction machinery is uniquely flexible. It is a transducer of three odorants—green pepper [15, 16], uroguanylin [13, 14] and CO 2 [18]; and it adopts itself to processing these odorants in multiple modes—through its extracellular, intracellular, Ca 2+ -dependent and Ca 2+ -independent modes.…”

Section: Discussionmentioning

confidence: 99%

“…Membrane fractions of transfected COS cells were assayed for guanylate cyclase activity as described previously [14, 15, 17]. Briefly, membranes were incubated on ice with NaHCO 3 and/or neurocalcin δ in the assay system containing 10 mM theophylline, 15 mM phosphocreatine, 20 μg creatine kinase and 50 mM Tris-HCl, pH 7.5, adjusted to 10 μM free Ca 2+ or 1 mM EGTA concentrations with pre-calibrated Ca 2+ /EGTA solutions (Molecular Probes).…”

Section: Methodsmentioning

confidence: 99%

“…In contrast to the cyclic AMP, cyclic GMP pathway does not function through the GTP-binding protein, G olf . It directly originates from ONE-GC, which is both the receptor for the odorants uroguanylin [13, 14] and green pepper [15, 16], and also the transducer through its guanylate cyclase activity. Thus, on the lines of the prototype model of ANF-RGC membrane guanylate cyclase signal transduction [17], coexistence of the uroguanylin receptor and guanylate cyclase activities on a single transmembrane spanning polypeptide chain demonstrates that the mechanism of signal transduction involving mediation by the second messenger, cyclic GMP, is different from the adenylate cyclase system.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO2

Duda

Sharma

2010

Biochemical and Biophysical Research Communications

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In a subset of the olfactory sensory neurons ONE-GC$ membrane guanylate cyclase is a central component of two odorant-dependent cyclic GMP signaling pathways. These odorants are uroguanylin and CO2. The present study was designed to decipher the biochemical and molecular differences between these two odorant signaling mechanisms. The study shows (1) in contrast to uroguanylin, CO2 transduction mechanism is Ca2+-independent. (2) CO2 transduction site, like that of uroguanylin-neurocalcin δ, resides in the core catalytic domain, aa 880-1028, of ONE-GC. (3) The site, however, does not overlap the signature neurocalcin δ signal transduction domain, 908LSEPIE913. Finally, (4) this study negates the prevailing concept that CO2 uniquely signals ONE-GC activity [Sun, L. et al., (2009) Proc. Natl. Acad. Sci. USA. 106, 2041-2046; Guo, D. et al., (2009) Biochemistry 48, 4417-4422]. It demonstrates that it also signals the activation of photoreceptor membrane guanylate cyclase ROS-GC1. These results show an additional new transduction mechanism of the membrane guanylate cyclases and broaden our understanding of the molecular mechanisms by which different odorants using a single guanylate cyclase can regulate diverse cyclic GMP signaling pathways.

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Section: Resultssupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO2

Duda

Sharma

2010

Biochemical and Biophysical Research Communications

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“…A guanylyl cyclase activity present in cultured OSNs and in membrane preparations containing OSN cilia could be activated by Ca 2+ and GCAP1 [13] or by hippocalcin [28]. Subsequent studies of heterologously expressed GC-D (as well as of membrane preparations isolated from MOE) have implicated GCAP1, the myristolated form of neurocalcin δ , and hippocalcin in the Ca 2+ -dependent activation of this particular guanylyl cyclase [29–33]. Both groups concluded that regulation of receptor guanylyl cyclases by Ca 2+ -binding proteins provides an opportunity to amplify or otherwise impact the canonical odor-dependent cAMP signaling cascade [e.g., 13, 22].…”

Section: Modulation Of Gc-d Activity By Intracellular Signalsmentioning

confidence: 99%

Receptor guanylyl cyclases in mammalian olfactory function

Zufall

Munger

2009

Mol Cell Biochem

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The contributions of guanylyl cyclases to sensory signaling in the olfactory system have been unclear. Recently, studies of a specialized subpopulation of olfactory sensory neurons (OSNs) located in the main olfactory epithelium have provided important insights into the neuronal function of one receptor guanylyl cyclase, GC-D. Mice expressing reporters such as β-galactosidase and green fluorescent protein in OSNs that normally express GC-D have allowed investigators to identify these neurons in situ, facilitating anatomical and physiological studies of this sparse neuronal population. The specific perturbation of GC-D function in vivo has helped to resolve the role of this guanylyl cyclase in the transduction of olfactory stimuli. Similar approaches could be useful for the study of the orphan receptor GC-G, which is expressed in another distinct subpopulation of sensory neurons located in the Grueneberg ganglion. In this review, we discuss key findings that have reinvigorated the study of guanylyl cyclase function in the olfactory system.

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Visinin-like proteins (VSNLs): interaction partners and emerging functions in signal transduction of a subfamily of neuronal Ca2+-sensor proteins

2008

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The visinin-like protein (VSNL) subfamily, including the founder protein VILIP-1, VILIP-2, VILIP-3, hippocalcin and neurocalcin δ, constitute a highly homologous subfamily of neuronal calcium sensor (NCS) proteins. Comparative studies have shown that VSNLs are expressed predominantly in the brain with restricted expression patterns in different subsets of neurons, but are also found in peripheral organs. In addition, the proteins display differences in their calcium affinities, their membrane binding kinetics and in the intracellular targets to which they associate after calcium binding. Even though the proteins use a similar calcium-myristoyl switch mechanism to translocate to cellular membranes, they show calcium-dependent localization to different subcellular compartments when expressed in the same neuron. These distinct calcium-myristoyl switch properties might be explained by specificity for defined phospholipids and membrane-bound targets, which enable VSNLs to modulate various cellular signal transduction pathways, including cyclic nucleotide and MAPK signaling. An emerging theme is the direct or indirect effect of VSNLs on gene expression and the interaction with components of membrane trafficking complexes which may determine a role in membrane trafficking of different receptors and ion channels, such as glutamate receptors of the kainate and AMPA subtype, nicotinic ACh receptors and Ca2+-channels. One hypothesis is that the highly homologous VSNLs have evolved to fulfill specialized functions in membrane trafficking and thereby affect neuronal signaling and differentiation in defined subsets of neurons. VSNLs are involved in differentiation processes showing a tumor invasion suppressor function in peripheral organs. Finally, VSNLs play neuroprotective and neurotoxic roles and have been implicated in neurodegenerative diseases.

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Calcium-modulated ciliary membrane guanylate cyclase transduction machinery: Constitution and operational principles

Cited by 14 publications

References 43 publications

Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO2

Distinct ONE-GC transduction modes and motifs of the odorants: Uroguanylin and CO2

Receptor guanylyl cyclases in mammalian olfactory function

Visinin-like proteins (VSNLs): interaction partners and emerging functions in signal transduction of a subfamily of neuronal Ca2+-sensor proteins

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