Nuclear actin: ancient clue to evolution in eukaryotes?
- 319 Downloads
Until recently it was widely accepted that the dynamic cytoskeletal matrix is exclusive to the cytoplasm of eukaryotes, evolving before the emergence of the cell nucleus to enable phagocytosis, cell motility and the sophisticated functioning of the endomembrane system within the cytosol. The discovery of the existence of a prokaryotic cytoskeleton has changed this picture significantly. As a result, the idea has taken shape that the appearance of actin occurred in the very first cell; therefore, the emergence of microfilaments precedes that of the eukaryotic cytoskeleton. The discovery of nuclear actin opened new perspective on the field, suggesting that the nuclear activities of actin reflect the functions of primordial actin-like proteins. In this paper, we review the recent literature to explore the evolutionary origin of nuclear actin. We conclude that both ancient and eukaryotic features of the actin world can be detected in the nucleus today, which supports the idea that the cytoskeleton attained significant eukaryotic innovations before the tandem evolution of the cytoskeleton and nucleus occurred.
KeywordsActin Evolution Cytoskeleton Nucleus
Nuclear pore complex
Linker of nucleoskeleton and cytoskeleton
Nuclear localization signal
Serum response factor
Megakaryoblastic leukemia protein 1
Inner nuclear membrane protein
The authors acknowledge Miklós Erdélyi, József Mihály and Gabriel Fenteany (BRC Szeged) for the critical reading of the manuscript.
This work was supported by the National Research, Development and Innovation Office—NKFIH (GINOP-2.3.2-15-2016-00001, GINOP-2.3.2-15-2016-00032 and PD127968).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
- Baarlink C, Plessner M, Sherrard A, Morita K, Misu S, Virant D, Kleinschnitz EM, Harniman R, Alibhai D, Baumeister S, Miyamoto K, Endesfelder U, Kaidi A, Grosse R (2017) A transient pool of nuclear F-actin at mitotic exit controls chromatin organization. Nat Cell Biol 19(12):1389–1399. https://doi.org/10.1038/ncb3641 PubMedCrossRefGoogle Scholar
- Hofmann WA, Stojiljkovic L, Fuchsova B, Vargas GM, Mavrommatis E, Philimonenko V, Kysela K, Goodrich JA, Lessard JL, Hope TJ, Hozak P, de Lanerolle P (2004) Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat Cell Biol 6:1094–1101PubMedCrossRefGoogle Scholar
- Jiang S, Narita A, Popp D, Ghoshdastider U, Lee LJ, Srinivasan R, Balasubramanian MK, Oda T, Koh F, Larsson M, Robinson RC (2016) Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation. Proc Natl Acad Sci USA 113(9):E1200–E1205. https://doi.org/10.1073/pnas.1600129113 PubMedCrossRefGoogle Scholar
- Reyes A, He J, Mao CC, Bailey LJ, Di Re M, Sembongi H, Kazak L, Dzionek K, Holmes JB, Cluett TJ, Harbour ME, Fearnley IM, Crouch RJ, Conti MA, Adelstein RS, Walker JE, Holt IJ (2011) Actin and myosin contribute to mammalian mitochondrial DNA maintenance. Nucleic Acids Res 39(12):5098–5108. https://doi.org/10.1093/nar/gkr052 PubMedPubMedCentralCrossRefGoogle Scholar
- Serebryannyy LA, Parilla M, Annibale P, Cruz CM, Laster K, Gratton E, Kudryashov D, Kosak ST, Gottardi CJ, de Lanerolle P (2016a) Persistent nuclear actin filaments inhibit transcription by RNA polymerase II. J Cell Sci 129(18):3412–3425. https://doi.org/10.1242/jcs.195867 PubMedPubMedCentralCrossRefGoogle Scholar
- Straub FB (1942) Actin. Stud Inst Med Chem Univ Szeged 2:3–15. http://actin.aok.pte.hu/archives/pdf/StudiesII_1.pdf. Accessed 28 Feb 2018