Membrane guanylate cyclase is a beautiful signal transduction machine: overview

Sharma, Rameshwar K.

doi:10.1007/s11010-009-0336-6

Cited by 41 publications

(104 citation statements)

References 266 publications

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“…The original discovery of the photoreceptor ROS-GC system revealed several unusual signaling features (reviewed in [1,34,35] dissociates from GCAPs, whereupon GCAPs markedly increase ROS-GC activity. This restorative effect on cyclic GMP levels sets the operating range of light intensities under dark and light adapted conditions, accelerates the photoresponse recovery, and suppresses continuous noise due to basal phosphodiesterase activity [16,42].…”

Section: Discussionmentioning

confidence: 99%

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Wen

Duda²,

Pertzev³

et al. 2012

Cell Physiol Biochem

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Rod outer segment membrane guanylate cyclase (ROS-GC1) is a bimodal Ca²⁺ signal transduction switch. Lowering [Ca²⁺]_i from 200 to 20 nM progressively turns it “ON” as does raising [Ca²⁺]_i from 500 to 5000 nM. The mode operating at lower [Ca²⁺]_i plays a vital role in phototransduction in both rods and cones. The physiological function of the mode operating at elevated [Ca²⁺]_i is not known. Through comprehensive studies on mice involving gene deletions, biochemistry, immunohistochemistry, electroretinograms and single cell recordings, the present study demonstrates that the Ca²⁺-sensor S100B coexists with and is physiologically linked to ROS-GC1 in cones but not in rods. It up-regulates ROS-GC1 activity with a K_1/2 for Ca²⁺ greater than 500 nM and modulates the transmission of neural signals to cone ON-bipolar cells. Furthermore, a possibility is raised that under pathological conditions where [Ca²⁺]_i levels rise to and perhaps even enter the micromolar range, the S100B signaling switch will be turned “ON” causing an explosive production of CNG channel opening and further rise in [Ca²⁺]_i in cone outer segments. The findings define a new cone-specific Ca²⁺-dependent feature of photoreceptors and expand our understanding of the operational principles of phototransduction machinery.

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Section: Discussionmentioning

confidence: 99%

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Wen

Duda²,

Pertzev³

et al. 2012

Cell Physiol Biochem

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“…It favored the hormonal second messenger role of cyclic GMP (reviewed in Sharma, 2010). Studies with the model systems of the isolated adrenal fasciculata and the adrenocortical carcinoma cells established a membrane guanylate cyclase to be the direct and specific transducer of the adrenocorticotropic hormone (ACTH).…”

Section: History: Year 1963–1987mentioning

confidence: 99%

“…It then moves on to its present status. To make the presentation simple and chronologically continuous, the subject matters of the earlier reviews (Sharma et al, 1997; Pugh et al, 1997; Sharma, 2002; Duda et al, 2005b; Sharma, 2010; Sharma and Duda, 2012) and publication of these authors have been freely borrowed with appropriate citations.…”

Section: Introductionmentioning

confidence: 99%

Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions

Sharma

Duda

2014

Front. Mol. Neurosci.

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A sequel to these authors' earlier comprehensive reviews which covered the field of mammalian membrane guanylate cyclase (MGC) from its origin to the year 2010, this article contains 13 sections. The first is historical and covers MGC from the year 1963–1987, summarizing its colorful developmental stages from its passionate pursuit to its consolidation. The second deals with the establishment of its biochemical identity. MGC becomes the transducer of a hormonal signal and founder of the peptide hormone receptor family, and creates the notion that hormone signal transduction is its sole physiological function. The third defines its expansion. The discovery of ROS-GC subfamily is made and it links ROS-GC with the physiology of phototransduction. Sections ROS-GC, a Ca2+-Modulated Two Component Transduction System to Migration Patterns and Translations of the GCAP Signals Into Production of Cyclic GMP are Different cover its biochemistry and physiology. The noteworthy events are that augmented by GCAPs, ROS-GC proves to be a transducer of the free Ca2+ signals generated within neurons; ROS-GC becomes a two-component transduction system and establishes itself as a source of cyclic GMP, the second messenger of phototransduction. Section ROS-GC1 Gene Linked Retinal Dystrophies demonstrates how this knowledge begins to be translated into the diagnosis and providing the molecular definition of retinal dystrophies. Section Controlled By Low and High Levels of [Ca2+]i, ROS-GC1 is a Bimodal Transduction Switch discusses a striking property of ROS-GC where it becomes a “[Ca2+]i bimodal switch” and transcends its signaling role in other neural processes. In this course, discovery of the first CD-GCAP (Ca2+-dependent guanylate cyclase activator), the S100B protein, is made. It extends the role of the ROS-GC transduction system beyond the phototransduction to the signaling processes in the synapse region between photoreceptor and cone ON-bipolar cells; in section Ca2+-Modulated Neurocalcin δ ROS-GC1 Transduction System Exists in the Inner Plexiform Layer (IPL) of the Retinal Neurons, discovery of another CD-GCAP, NCδ, is made and its linkage with signaling of the inner plexiform layer neurons is established. Section ROS-GC Linkage With Other Than Vision-Linked Neurons discusses linkage of the ROS-GC transduction system with other sensory transduction processes: Pineal gland, Olfaction and Gustation. In the next, section Evolution of a General Ca2+-Interlocked ROS-GC Signal Transduction Concept in Sensory and Sensory-Linked Neurons, a theoretical concept is proposed where “Ca2+-interlocked ROS-GC signal transduction” machinery becomes a common signaling component of the sensory and sensory-linked neurons. Closure to the review is brought by the conclusion and future directions.

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“…Its discovery and molecular characterization was a land mark event in the field of phototransduction (reviewed in Pugh et al, 1997; Koch et al, 2010) as it identified the source of cyclic GMP that serves as a second messenger of the LIGHT signal. It also impacted the entire membrane guanylate cyclase field by dividing the guanylate cyclase family into two subfamilies, one comprising the hormone receptor cyclases, and the other, cyclases modulated by intracellular [Ca 2+ ] i signals (reviewed in: Sharma, 2010). ROS-GC1 belongs to the second subfamily together with another rod outer segment guanylate cyclase ROS-GC2 (Ret-GC2 or GC-F), and the olfactory neuroepithelial guanylate cyclase, ONE-GC (GC-D; reviewed in: Sharma, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…It also impacted the entire membrane guanylate cyclase field by dividing the guanylate cyclase family into two subfamilies, one comprising the hormone receptor cyclases, and the other, cyclases modulated by intracellular [Ca 2+ ] i signals (reviewed in: Sharma, 2010). ROS-GC1 belongs to the second subfamily together with another rod outer segment guanylate cyclase ROS-GC2 (Ret-GC2 or GC-F), and the olfactory neuroepithelial guanylate cyclase, ONE-GC (GC-D; reviewed in: Sharma, 2010). …”

Section: Introductionmentioning

confidence: 99%

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

Jankowska

Sharma

Duda

2014

Front. Mol. Neurosci.

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ROS-GC1 belongs to the Ca2+-modulated sub-family of membrane guanylate cyclases. It primarily exists and is linked with signaling of the sensory neurons – sight, smell, taste, and pinealocytes. Exceptionally, it is also present and is Ca2+-modulated in t he non-neuronal cells, the sperm cells in the testes, where S100B protein serves as its Ca2+ sensor. The present report demonstrates the identification of an additional Ca2+ sensor of ROS-GC1 in the testes, neurocalcin δ. Through mouse molecular genetic models, it compares and quantifies the relative input of the S100B and neurocalcin δ in regulating the Ca2+ signaling of ROS-GC1 transduction machinery, and via immunochemistry it demonstrates the co-presence of neurocalcin δ and ROS-GC1 in the spermatogenic cells of the testes. The suggestion is that in more ways than one the Ca2+-modulated ROS-GC1 transduction system is linked with the testicular function. This non-neuronal transduction system may represent an illustration of the ROS-GC1 expanding role in the trans-signaling of the neural and non-neural systems.

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Membrane guanylate cyclase is a beautiful signal transduction machine: overview

Cited by 41 publications

References 266 publications

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

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Membrane guanylate cyclase is a beautiful signal transduction machine: overview

Cited by 41 publications

References 266 publications

S100B Serves as a Ca2+Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca2+Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions

Ca2+-modulated ROS-GC1 transduction system in testes and its presence in the spermatogenic cells

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S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina

S100B Serves as a Ca²⁺Sensor for ROS-GC1 Guanylate Cyclase in Cones but not in Rods of the Murine Retina