Cryptic Enzymes and Moonlighting Proteins

1st Edition - May 2, 2025
Imprint: Academic Press
Editors: Helen Irving, Chris Gehring, Aloysius Wong
Language: English
Paperback ISBN:
9 7 8 - 0 - 4 4 3 - 1 5 7 1 9 - 6
eBook ISBN:
9 7 8 - 0 - 4 4 3 - 1 5 7 2 0 - 2

Cryptic Enzymes and Moonlighting Proteins, a new volume in the Foundations and Frontiers in Enzymology series, offers a thorough overview of cryptic enzymes and moonlighting… Read more

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Cryptic Enzymes and Moonlighting Proteins, a new volume in the Foundations and Frontiers in Enzymology series, offers a thorough overview of cryptic enzymes and moonlighting proteins in signaling cascades. In early chapters, leading international contributors discuss evolutionary considerations for moonlighting proteins, moonlighting interactions in the extracellular matrix, eukaryotic moonlighting proteins, modulating, moonlighting kinases, moonlighting proteins in neurobiology signaling, metabolic enzymes moonlighting as RNA binding and regulatory proteins. Later, methods-driven chapters discuss practical aspects of identifying hidden moonlighting domains in proteins, computational approaches and bioinformatic tools for the identification of cryptic enzymes, establishing cryptic enzyme interactomes, and assessing contributions of moonlighting proteins to signal cascades.

The book also explores recent advances in research and brings together an array of information across different fields to enable better targeting of these exciting proteins and their interactomes. With a clear focus on the role of moonlighting and cryptic enzymes in signal transduction, users will find examples of cryptic enzymes across species, as well as those in human healthy biology and pathogenesis.

Title of Book
Cover image
Title page
Table of Contents
Copyright
List of contributors
About the editors
Preface
Chapter 1 Introduction and overview of moonlighting enzymes in signal cascades
Abstract
1.1 Introduction to moonlighting proteins
1.2 Intracellular proteins moonlighting in extracellular signaling
1.3 Moonlighting proteins in intracellular signaling
1.4 Moonlighting protein evolution
1.5 Discovering moonlighting proteins
1.6 Protein function prediction and cryptic functional domains
1.7 Summary
References
Chapter 2 Extracellular vesicles enabling moonlighting proteins
Abstract
2.1 Introduction
2.2 Extracellular vesicles
2.3 Extracellular vesicles containing moonlighting proteins
2.4 Conclusion
References
Chapter 3 Moonlighting proteins in neurobiology signaling mediated by G protein-coupled receptors
Abstract
3.1 Introduction
3.2 G protein–coupled receptors as moonlighting proteins
3.3 G protein–coupled receptors heteroreceptor complexes and their receptor–receptor interactions
3.4 Methods for studying receptor–receptor interactions and receptor–proteins interactions
3.5 G protein–coupled receptors heteroreceptor complexes and their interface interactions
3.6 Protomers in heteroreceptor complexes can act as moonlighting proteins via intermolecular receptor–receptor interactions or receptor–proteins interactions
3.7 Moonlighting G protein–coupled receptors provides opportunities as well as challenges for drug development
3.8 Conclusions
Funding
Conflicts of Interest
AI Disclosure
References
Chapter 4 Metabolic enzymes co-opted in oncogenic signalling
Abstract
4.1 Introduction
4.2 Hexokinase
4.3 Phosphofructokinase
4.4 Fructose-1,6-bisphosphatase
4.5 Aldolase
4.6 Concluding remarks
References
Chapter 5 Metabolic enzymes moonlighting as RNA binding and regulatory proteins
Abstract
5.1 Introduction and definitions of moonlighting proteins
5.2 Effects of enzyme–RNA interactions
5.3 Factors affecting enzyme binding to RNA
5.4 Affecting enzyme function
5.5 Many other enzymes also moonlight as non-canonical RNA binding proteins
5.6 Structures of RNA binding domains or regions
5.7 Conclusions
Acknowledgements
References
Chapter 6 Cryptic enzymes as fine tuners of signaling cascades
Abstract
6.1 Definition of cryptic enzymes
6.2 In search of cryptic enzymes—the case of guanylate cyclases in plants
6.3 How do cryptic enzymes do what they do—biochemistry and cell biology
6.4 PSKR1 and KUP5 as points in case
6.5 Cryptic enzymes as fine tuners of signal networks
6.6 Applications of motif searches beyond cryptic enzymes
6.7 Conclusions
References
Chapter 7 Dual function plant cryptic nucleotide cyclases
Abstract
7.1 Introduction
7.2 The long road to the discovery of nucleotide cyclases
7.3 Moonlighting/cryptic guanylate cyclases
7.4 Moonlighting/cryptic adenylate cyclases
7.5 Conclusions
References
Chapter 8 Crypto adenylate cyclases coming of age
Abstract
8.1 Introduction
8.2 A brief summary of cAMP detection in higher plants
8.3 The discovery of the first adenylate cyclases in higher plants
8.4 Crypto-adenylate cyclases as cyclases hidden in complex plant proteins
8.5 Summary
References
Chapter 9 Crypto adenylate cyclases moonlighting with phosphodiesterases in complex proteins
Abstract
9.1 Introduction
9.2 Roles and structure of phosphodiesterases
9.3 The path to the discovery of the plant phosphodiesterases
9.4 Twin cyclase–phosphodiesterase architecture
9.5 Outlook
References
Chapter 10 Gas-sensing H-NOX hemoproteins in plants and beyond
Abstract
10.1 Gas sensing
10.2 Finding heme-nitric oxide/oxygen binding centers in proteins across the tree of life
10.3 Recently reported plant heme-nitric oxide/oxygen moonlighting proteins
10.4 Modifications of the heme-nitric oxide/oxygen motif and moonlighting proteins
10.5 Functional aspects of heme-nitric oxide/oxygen cassettes in complex moonlighting proteins
10.6 The search for heme-nitric oxide/oxygen moonlighting proteins beyond the plant kingdom
10.7 Conclusion
References
Chapter 11 Modulating the immune response via cryptic enzymes
Abstract
11.1 Innate immunity
11.2 Inflammation
11.3 The interleukin-1 receptor—associated kinase family
11.4 Interleukin-1 receptor-associated kinase-3
11.5 Guanylate cyclases
11.6 Interleukin-1 receptor-associated kinase-3 as a guanylate cyclase
11.7 Conclusions
References
Chapter 12 Cryptic moonlighting enzymes enable crosstalk with other signaling molecules
Abstract
12.1 Introduction
12.2 Pathogen attack can trigger cyclic nucleotide production by moonlighting enzymes
12.3 Damage-associated molecular pattern receptors and the production of cyclic nucleotides: PepRs
12.4 Damage-associated molecular patterns receptors and the production of cyclic nucleotides: PSKRs and possible crosstalk with brassinosteroid signaling
12.5 Damage-associated molecular pattern receptors and the production of cyclic nucleotides: wall-associated kinase-like and P2Ks
12.6 Crosstalk at the level of the protein
12.7 Future prospects
Acknowledgments
References
Chapter 13 Identifying hidden moonlighting proteins and protein regions
Abstract
13.1 Introduction
13.2 Databases of moonlighting proteins
13.3 Computational methods for finding moonlighting proteins
13.4 MPFit: detecting moonlighting proteins from omics data
13.5 Computational methods for prediction of disordered moonlighting regions
13.6 Conclusions
Acknowledgments
References
Chapter 14 Establishing cryptic enzyme interactomes
Abstract
14.1 Protein–protein interactions
14.2 Computational methods for prediction of cryptic enzymes’ protein–protein interactions
14.3 Biochemical methods used for detection of interactors of cryptic enzymes
14.4 Biophysical protein–protein interaction methods used for detection of interactors of cryptic enzymes
14.5 Genetic approaches to investigation of cryptic enzymes’ protein–protein interactions
14.6 Conclusions
References
Chapter 15 Nucleotidyl cyclase activities of TIR1/AFB auxin receptors: new insights into the mechanism of auxin signaling
Abstract
15.1 Introduction
15.2 Discovery of TIR1/AFB-mediated canonical auxin signaling pathway
15.3 Emergence of TIR1/AFB-mediated nontranscriptional signaling branch
15.4 TIR1/AFBs have both adenylate cyclase and guanylate cyclase activities
15.5 Auxin perception stimulates the adenylate cyclase and guanylate cyclase activities of TIR1/AFBs
15.6 TIR1 adenylate cyclase activity is crucial for canonical transcriptional responses
15.7 AFB1 guanylate cyclase activity is involved in rapid, nontranscriptional auxin responses
15.8 Conclusions and perspectives
References
Chapter 16 Uncovering moonlighting proteins in cell organelles
Abstract
16.1 Moonlighting protein function association with its subcellular localization
16.2 Protein localization to subcellular compartments
16.3 Computational approaches to the identification of moonlighting protein location
16.4 Computational identification of subcellular targeting signals
16.5 Visualization of intracellular proteins
16.6 Isolation of subcellular compartments for visualization and functional analysis of proteins
16.7 Conclusions
References
Index

Helen Irving

Helen Irving is a Professor in Biomedical Sciences and is a member of the La Trobe Institute for Molecular Sciences (LIMS) in Melbourne, Australia. Helen's current research centers on understanding inflammatory signals at the molecular level to develop new and improved approaches to managing inflammatory conditions. Helen obtained her PhD in Biochemistry from The University of Melbourne and conducted post-doctoral work at Vanderbilt University (USA) and The University of Kentucky (USA) before returning to Australia to take up an ARC Post-Doctoral Fellowship at La Trobe University. For most of her career, she has been a teaching and research academic based at the Faculty of Pharmacy and Pharmaceutical Sciences at Monash University. Helen moved to the La Trobe Institute for Molecular Sciences (LIMS) at La Trobe University in 2017.

Affiliations and expertise

Professor in Biomedical Sciences, La Trobe Institute for Molecular Sciences (LIMS), Melbourne, Australia

Chris Gehring

Dr. Chris Gehring is based at the Università degli Studi di Perugia UNIPG, in the Department of Chemistry, Biology & Biotechnology. His research focuses on plant signalling peptides, with a focus on various peptide signalling molecules in development, defense, and homeostasis. He has published widely in such peer reviewed journals as Nature, Molecular Plant, Trends in Genetics, and the Journal of Biological Chemistry.

Affiliations and expertise

Professor, Department of Chemistry, Biology and Biotechnology, Università degli Studi di Perugia UNIPG, Italy

Aloysius Wong

Dr. Aloysius Wong earned a PhD in Bioscience from King Abdullah University of Science and Technology (KAUST), Saudi Arabia, as well as a MA in Biotechnology from the University of Cambridge, UK. In past positions, he has served as a post-doctoral researcher at the French National Centre for Scientific Research. Dr. Wong seeks to understand, from a molecular perspective, how plants, despite being sessile and immobile, can efficiently perceive environmental (biotic and abiotic) signals and launch short- and long-term biological responses that enable them to survive in environments considered hostile to plants. Dr. Wong has published widely in peer reviewed journals.

Affiliations and expertise

Assistant Professor, Wenzhou-Kean University, Wenzhou, China

Life Sciences

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Cryptic Enzymes and Moonlighting Proteins

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Helen Irving

Chris Gehring

Aloysius Wong

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