Functional diversification of centrins and cell morphological complexity
- PMID: 18057024
- DOI: 10.1242/jcs.019414
Functional diversification of centrins and cell morphological complexity
Abstract
In addition to their key role in the duplication of microtubule organising centres (MTOCs), centrins are major constituents of diverse MTOC-associated contractile arrays. A centrin partner, Sfi1p, has been characterised in yeast as a large protein carrying multiple centrin-binding sites, suggesting a model for centrin-mediated Ca2+-induced contractility and for the duplication of MTOCs. In vivo validation of this model has been obtained in Paramecium, which possesses an extended contractile array - the infraciliary lattice (ICL) - essentially composed of centrins and a huge Sfi1p-like protein, PtCenBP1p, which is essential for ICL assembly and contractility. The high molecular diversity revealed here by the proteomic analysis of the ICL, including ten subfamilies of centrins and two subfamilies of Sf1p-like proteins, led us to address the question of the functional redundancy, either between the centrin-binding proteins or between the centrin subfamilies. We show that all are essential for ICL biogenesis. The two centrin-binding protein subfamilies and nine of the centrin subfamilies are ICL specific and play a role in its molecular and supramolecular architecture. The tenth and most conserved centrin subfamily is present at three cortical locations (ICL, basal bodies and contractile vacuole pores) and might play a role in coordinating duplication and positioning of cortical organelles.
Similar articles
-
An Sfi1p-like centrin-binding protein mediates centrin-based Ca2+ -dependent contractility in Paramecium tetraurelia.Eukaryot Cell. 2007 Nov;6(11):1992-2000. doi: 10.1128/EC.00197-07. Epub 2007 Aug 3. Eukaryot Cell. 2007. PMID: 17675401 Free PMC article.
-
Centrin deficiency in Paramecium affects the geometry of basal-body duplication.Curr Biol. 2005 Dec 6;15(23):2097-106. doi: 10.1016/j.cub.2005.11.038. Curr Biol. 2005. PMID: 16332534
-
Centrin is a conserved protein that forms diverse associations with centrioles and MTOCs in Naegleria and other organisms.Cell Motil Cytoskeleton. 1996;33(4):298-323. doi: 10.1002/(SICI)1097-0169(1996)33:4<298::AID-CM6>3.0.CO;2-5. Cell Motil Cytoskeleton. 1996. PMID: 8801035
-
Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1.Vision Res. 2006 Dec;46(27):4568-74. doi: 10.1016/j.visres.2006.07.034. Epub 2006 Oct 6. Vision Res. 2006. PMID: 17027898 Review.
-
A mechanistic view on the evolutionary origin for centrin-based control of centriole duplication.J Cell Physiol. 2007 Nov;213(2):420-8. doi: 10.1002/jcp.21226. J Cell Physiol. 2007. PMID: 17694534 Review.
Cited by
-
Outer dynein arm light chain 1 is essential for controlling the ciliary response to cyclic AMP in Paramecium tetraurelia.Eukaryot Cell. 2012 May;11(5):645-53. doi: 10.1128/EC.05279-11. Epub 2012 Mar 16. Eukaryot Cell. 2012. PMID: 22427431 Free PMC article.
-
Multimerization properties of PiggyMac, a domesticated piggyBac transposase involved in programmed genome rearrangements.Nucleic Acids Res. 2017 Apr 7;45(6):3204-3216. doi: 10.1093/nar/gkw1359. Nucleic Acids Res. 2017. PMID: 28104713 Free PMC article.
-
Sfr13, a member of a large family of asymmetrically localized Sfi1-repeat proteins, is important for basal body separation and stability in Tetrahymena thermophila.J Cell Sci. 2013 Apr 1;126(Pt 7):1659-71. doi: 10.1242/jcs.120238. Epub 2013 Feb 20. J Cell Sci. 2013. PMID: 23426847 Free PMC article.
-
The transient Spt4-Spt5 complex as an upstream regulator of non-coding RNAs during development.Nucleic Acids Res. 2022 Mar 21;50(5):2603-2620. doi: 10.1093/nar/gkac106. Nucleic Acids Res. 2022. PMID: 35188560 Free PMC article.
-
Differential localization and functional specialization of centrin analogs in the parasitic ciliate Trichodina pediculus.Protoplasma. 2016 Sep;253(5):1385-8. doi: 10.1007/s00709-015-0878-2. Epub 2015 Sep 4. Protoplasma. 2016. PMID: 26340903
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous