Enzyme filaments are defined as reversible, functional, linear self-assemblies of a single type of enzyme. Filamentation has recently emerged as a new mode of enzymatic regulation. In this Comment, we briefly introduce the diversity and functional consequences of enzyme filamentation.
This is a preview of subscription content, access via your institution
Relevant articles
Open Access articles citing this article.
-
Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex
Nature Microbiology Open Access 15 July 2021
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 / 30 days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Kleinschmidt, A. K., Moss, J. & Lane, D. M. Acetyl coenzyme A carboxylase: filamentous nature of the animal enzymes. Science 166, 1276–1278 (1969).
Narayanaswamy, R. et al. Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation. Proc. Natl Acad. Sci. USA 106, 10147–10152 (2009).
Noree, C. et al. Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster. J. Cell Biol. 190, 541–551 (2010).
Lynch, E. M. et al. Human CTP synthase filament structure reveals the active enzyme conformation. Nat. Struct. Mol. Biol. 24, 507–514 (2017).
Hunkeler, M. et al. Structural basis for regulation of human acetyl-CoA carboxylase. Nature 558, 470–474 (2018).
Polley, S., Lyumkis, D. & Horton, N. C. Mechanism of filamentation-induced allosteric activation of the SgrAI endonuclease. Structure 27, 1497–1507 (2019).
Park, C. K. & Horton, N. C. Structure, function, and mechanism of filament forming enzymes: a renaissance of enzyme filamentation. Biophys. Rev. https://doi.org/10.1007/s12551-019-00602-6 (2019).
Angelucci, F. et al. Switching between the alternative structures and functions of a 2-Cys peroxiredoxin, by site-directed mutagenesis. J. Mol. Biol. 425, 4556–4568 (2013).
Yin, Q. et al. Structural biology of innate immunity. Annu. Rev. Immunol. 33, 393–416 (2015).
Barahona, C. J. et al. The need for speed: run-on oligomer filament formation provides maximum speed with maximum sequestration of activity. J. Virol. 93, 1–19 (2019).
Acknowledgements
N.C.H. is supported by the National Science Foundation, grant numbers MCB-1410355 and MCB-1934291.
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The authors declare no competing interests.
Additional information
Publisher’s note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Park, C.K., Horton, N.C. Novel insights into filament-forming enzymes. Nat Rev Mol Cell Biol 21, 1–2 (2020). https://doi.org/10.1038/s41580-019-0188-1
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41580-019-0188-1