Understanding protein multifunctionality: from short linear motifs to cellular functions

Moonlighting proteins perform multiple unrelated functions without any change in polypeptide sequence. They can coordinate cellular activities, serving as switches between pathways and helping to respond to changes in the cellular environment. Therefore, regulation of the multiple protein activities...

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Veröffentlicht in:Cellular and molecular life sciences : CMLS Jg. 76; H. 22; S. 4407 - 4412
Hauptverfasser: Zanzoni, Andreas, Ribeiro, Diogo M., Brun, Christine
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Cham Springer International Publishing 01.11.2019
Springer Nature B.V
Springer Verlag
Schlagworte:
Animals
Biochemistry
Biochemistry, Molecular Biology
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cell Physiological Phenomena - physiology
Databases, Protein
Enzymes
Gene expression
Homeostasis
Humans
Life Sciences
Localization
Molecular biology
Moonlighting
Polypeptides
Protein Conformation
Proteins
Proteins - metabolism
Quantitative Methods
Review
space and time
Switches
Protein interaction networks
Molecular switch
Multifunctional proteins
Cell signalling regulation
Short linear motifs
Bioinformatics
Moonlighting proteins
ISSN:1420-682X, 1420-9071, 1420-9071
Online-Zugang:Volltext
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Zusammenfassung:Moonlighting proteins perform multiple unrelated functions without any change in polypeptide sequence. They can coordinate cellular activities, serving as switches between pathways and helping to respond to changes in the cellular environment. Therefore, regulation of the multiple protein activities, in space and time, is likely to be important for the homeostasis of biological systems. Some moonlighting proteins may perform their multiple functions simultaneously while others alternate between functions due to certain triggers. The switch of the moonlighting protein’s functions can be regulated by several distinct factors, including the binding of other molecules such as proteins. We here review the approaches used to identify moonlighting proteins and existing repositories. We particularly emphasise the role played by short linear motifs and PTMs as regulatory switches of moonlighting functions.
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ISSN:1420-682X
1420-9071
1420-9071
DOI:10.1007/s00018-019-03273-4