ArticleBiochemistry2010
Ca(2+) sensor GCAP1: A constitutive element of the ONE-GC-modulated odorant signal transduction pathway.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Multilimbed membrane guanylate cyclase signaling system, evolutionary ladder.Frontiers in molecular neuroscience · 2022Review
- COMolecular and cellular biochemistry · 2018Article
- Integrative Signaling Networks of Membrane Guanylate Cyclases: Biochemistry and Physiology.Frontiers in molecular neuroscience · 2016Review
- Bicarbonate and Ca(2+) Sensing Modulators Activate Photoreceptor ROS-GC1 Synergistically.Frontiers in molecular neuroscience · 2016Article
- Membrane guanylate cyclase, a multimodal transduction machine: history, present, and future directions.Frontiers in molecular neuroscience · 2014Review
- Atrial natriuretic factor receptor guanylate cyclase, ANF-RGC, transduces two independent signals, ANF and Ca(2+).Frontiers in molecular neuroscience · 2014Review
- Antithetical modes of and the Ca(2+) sensors targeting in ANF-RGC and ROS-GC1 membrane guanylate cyclases.Frontiers in molecular neuroscience · 2012Article
- 657WTAPELL663 motif of the photoreceptor ROS-GC1: a general phototransduction switch.Biochemical and biophysical research communications · 2011Article
- Allosteric modification, the primary ATP activation mechanism of atrial natriuretic factor receptor guanylate cyclase.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In a small subset of the olfactory sensory neurons, the odorant receptor ONE-GC guanylate cyclase is a central transduction component of the cyclic GMP signaling pathway. In a two-step transduction model, the odorant, uroguanylin, binds to the extracellular domain and activates its intracellular domain to generate the odorant second messenger, cyclic GMP. This study via comprehensive technology, including gene deletion, live cell Forster resonance energy transfer (FRET), and surface plasmon resonance (SPR) spectroscopy, documents the identity of a remarkably intriguing operation of a Ca(2+) sensor component of the ONE-GC transduction machinery, GCAP1. In the ciliary membranes, the sites of odorant transduction, GCAP1 is biochemically and physiologically coupled to ONE-GC. Strikingly, this coupling reverses its well- established function in ROS-GC1 signaling, linked with phototransduction. In response to the free Ca(2+) range from nanomolar to semimicromolar, it inhibits ROS-GC1, yet in this range, it incrementally stimulates ONE-GC. These two opposite modes of signaling two SENSORY processes by a single Ca(2+) sensor define a new transduction paradigm of membrane guanylate cyclases. This paradigm is pictorially presented.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.