A multifunctional calcium-binding protein, centrin-1, is specifically expressed in male germ cells, certain neurons and ciliated cells. We identified centrin-1 as a protein interacting with SUMO-2/3 using yeast two-hybrid screening of a mouse testicular cDNA library. In bead halo assays, the interaction between centrin-1 and SUMO-2/3 was reduced in the presence of EGTA and facilitated by the addition of CaCl₂. immunostaining of seminiferous tubules in 35-day-old mouse testes revealed that cells in the layer containing spermatogonia showed colocalization of SUMO-2/3 with centrin-1 in cytoplasmic spots. Identification of centrin-1 as the EGTA-sensitive SUMO-2/3-interacting protein indicates the possible role of calcium in modulating the centrin-1-SUMO-2/3 interaction and suggests the importance of this interaction in mouse testis.
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http://dx.doi.org/10.1002/cbf.1698 | DOI Listing |
Syst Biol Reprod Med
June 2023
Department Molecular and Developmental Medicine, University of Siena, Siena, Italy.
This review provides details on the role of centrin in human spermatozoa and in various forms of male infertility. Centrin is a calcium (Ca)-binding phosphoprotein that is located in the centrioles - which are typical structures of the sperm connecting piece and play a key role in centrosome dynamics during sperm morphogenesis - as well as in zygotes and early embryos during spindle assembly. In humans, three different centrin genes encoding three isoforms have been discovered.
View Article and Find Full Text PDFBiochim Biophys Acta Mol Cell Res
March 2023
Department of Molecular Medicine, Jamia Hamdard, New Delhi 110062, India. Electronic address:
Centrins are cytoskeletal proteins associated with the centrosomes or basal bodies in the eukaryotes. We previously reported the involvement of Centrin 1-3 proteins in cell division in the protozoan parasites Leishmania donovani and Trypanosoma brucei. Centrin4 and 5, unique to such parasites, had never been characterized in Leishmania parasite.
View Article and Find Full Text PDFJ Reprod Dev
February 2023
Laboratory of Reproductive Physiology, Graduate School of Environmental and Life Science, Okayama University, Okayama 700-8530, Japan.
The oviductal epithelium consists of ciliated and non-ciliated cells, and their numbers vary depending on the segment of the oviduct and stage of the estrous cycle. Compared with the ampulla, fewer cyclic changes in the number of the two types of cells occur in the isthmus. Recently, we have reported that the epithelium in the ampullary oviduct is composed of many types of cells during different translational/transcriptional states, and their numbers change during the estrous cycle.
View Article and Find Full Text PDFBiomolecules
August 2022
Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy.
Centrins are calcium (Ca)-binding proteins that are involved in many cellular functions including centrosome regulation. A known cellular target of centrins is SFI1, a large centrosomal protein containing multiple repeats that represent centrin-binding motifs. Recently, a protein homologous to yeast and mammalian SFI1, denominated TgSFI1, which shares SFI1-repeat organization, was shown to colocalize at centrosomes with centrin 1 from (TgCEN1).
View Article and Find Full Text PDFBiochem Biophys Res Commun
September 2021
CSIR-Centre for Cellular and Molecular Biology (CCMB), Hyderabad, India; Indian Institute of Science Education and Research (IISER) Berhampur, India. Electronic address:
Centrin-1, a Ca sensor protein of the centrin family is a crucial player for cell division in eukaryotes and plays a key role in the microtubule organising centre. Despite being regarded as a calcium sensor with a matched structure to calmodulin/troponin C, the protein undergoes mild changes in conformation and binds Ca with moderate affinity. We present an in-depth analysis of the Ca sensing by individual EF-hand motifs of centrin-1 and address unsolved questions of the rationales for moderate affinity and conformational transitions of the protein.
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