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183 results on '"Gehring, Chris"'

9. Moonlighting Crypto-Enzymes and Domains as Ancient and Versatile Signaling Devices.

Author

Turek, Ilona, Wong, Aloysius, Domingo, Guido, Vannini, Candida, Bracale, Marcella, Irving, Helen, and Gehring, Chris

Subjects
GUANYLATE cyclase, ADENYLATE cyclase, PLANT hormones, ABSCISIC acid, CYCLASES
Abstract

Increasing numbers of reports have revealed novel catalytically active cryptic guanylate cyclases (GCs) and adenylate cyclases (ACs) operating within complex proteins in prokaryotes and eukaryotes. Here we review the structural and functional aspects of some of these cyclases and provide examples that illustrate their roles in the regulation of the intramolecular functions of complex proteins, such as the phytosulfokine receptor (PSKR), and reassess their contribution to signal generation and tuning. Another multidomain protein, Arabidopsis thaliana K+ uptake permease (AtKUP5), also harbors multiple catalytically active sites including an N-terminal AC and C-terminal phosphodiesterase (PDE) with an abscisic acid-binding site. We argue that this architecture may enable the fine-tuning and/or sensing of K+ flux and integrate hormone responses to cAMP homeostasis. We also discuss how searches with motifs based on conserved amino acids in catalytic centers led to the discovery of GCs and ACs and propose how this approach can be applied to discover hitherto masked active sites in bacterial, fungal, and animal proteomes. Finally, we show that motif searches are a promising approach to discover ancient biological functions such as hormone or gas binding. [ABSTRACT FROM AUTHOR]

Published
2024
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10. Cyclic Nucleotide Monophosphates in Plants and Plant Signaling

Author

Marondedze, Claudius, Wong, Aloysius, Thomas, Ludivine, Irving, Helen, Gehring, Chris, Barrett, James E., Editor-in-chief, Flockerzi, Veit, Series editor, Frohman, Michael A., Series editor, Geppetti, Pierangelo, Series editor, Hofmann, Franz B., Series editor, Michel, Martin C., Series editor, Page, Clive P., Series editor, Rosenthal, Walter, Series editor, Wang, KeWei, Series editor, and Seifert, Roland, editor

Published
2017
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35. Additional file 2: of Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms

Author

Marondedze, Claudius, Thomas, Ludivine, Gehring, Chris, and Lilley, Kathryn

Abstract

Proteins identified as responsive to polyethylene glycol treatment. (A) RNA binding protein (AT1G60650), (B) Rotamase CYP1 (AT4G38740), (C) SWIB/MDM2 domain protein (AT2G35605), (D) Calcium binding EF hand (At calmodulin like 4, AT2G41100), (E) Stress-inducible protein (AT1G62740). Total soluble protein changes are represented by the grey bars and RNA-binding protein or mRNA-interacting protein changes by the black bars. The asterisk represents significantly (pÂ

Published
2019
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36. Additional file 3: of Changes in the Arabidopsis RNA-binding proteome reveal novel stress response mechanisms

Author

Marondedze, Claudius, Thomas, Ludivine, Gehring, Chris, and Lilley, Kathryn

Subjects
fungi, food and beverages
Abstract

Classical and non-classical RNA-binding domains in Arabidopsis thaliana drought stress responsive RBPs mined using pfam database. (A) Most represented classical RNA-binding domains. (B) Most represented non-classical RNA-binding domains. Bars in blue represent number of protein domains mined from differentially expressed drought responsive proteins compared to domains present in drought responsive time specific proteins in red. (PDF 33 kb)

Published
2019
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42. Moonlighting proteins and their role in the control of signaling microenvironments, as exemplified by cGMP and phytosulfokine receptor 1 (PSKR1)

Author

Irving, Helen R., Cahill, David M., Gehring, Chris, Irving, Helen R., Cahill, David M., and Gehring, Chris

Abstract

Signal generating and processing complexes and changes in concentrations of messenger molecules such as calcium ions and cyclic nucleotides develop gradients that have critical roles in relaying messages within cells. Cytoplasmic contents are densely packed, and in plant cells this is compounded by the restricted cytoplasmic space. To function in such crowded spaces, scaffold proteins have evolved to keep key enzymes in the correct place to ensure ordered spatial and temporal and stimulus-specific message generation. Hence, throughout the cytoplasm there are gradients of messenger molecules that influence signaling processes. However, it is only recently becoming apparent that specific complexes involving receptor molecules can generate multiple signal gradients and enriched microenvironments around the cytoplasmic domains of the receptor that regulate downstream signaling. Such gradients or signal circuits can involve moonlighting proteins, so called because they can enable fine-tune signal cascades via cryptic additional functions that are just being defined. This perspective focuses on how enigmatic activity of moonlighting proteins potentially contributes to regional intracellular microenvironments. For instance, the proteins associated with moonlighting proteins that generate cyclic nucleotides may be regulated by cyclic nucleotide binding directly or indirectly. In this perspective, we discuss how generation of cyclic nucleotide-enriched microenvironments can promote and regulate signaling events. As an example, we use the phytosulfokine receptor (PSKR1), discuss the function of its domains and their mutual interactions and argue that this complex architecture and function enhances tuning of signals in microenvironments.

Published
2018

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