과제정보
This research was funded by the National Natural Science Foundation of China (Nos. 31460580 and 32060733 to J.L.H; No. 31660637 to P.W.); Agricultural Joint Project of the Yunnan Province Science and Technology Department (No. 202401BD070001-004 to J.L.H.); Basic Research Key Project of Yunnan Province, China (No. 202501AS070041 to J.L.H.); Yunnan Provincial Department of Education Scientific Research Fund Project, China (No. 2024J0451 to P.W.); College Student Innovation and Entrepreneurship Training Program (No. S202210676062 to R.N.G.L.T.R.G.).
참고문헌
- Mostowy S, Cossart P. Septins: the fourth component of the cytoskeleton. Nat Rev Mol Cell Biol 2012;13:183-94. https://doi.org/10.1038/nrm3284
- Kuo YC, Shen YR, Chen HI, et al. SEPT12 orchestrates the formation of mammalian sperm annulus by organizing core octameric complexes with other SEPT proteins. J Cell Sci 2015;128:923-34. https://doi.org/10.1242/jcs.158998
- Lin YH, Lin YM, Wang YY, et al. The expression level of septin12 is critical for spermiogenesis. Am J Pathol 2009;174: 1857-68. https://doi.org/10.2353/ajpath.2009.080955
- Yeh CH, Kuo PL, Wang YY, et al. SEPT12/SPAG4/LAMINB1 complexes are required for maintaining the integrity of the nuclear envelope in postmeiotic male germ cells. PLOS ONE 2015;10:e0120722. https://doi.org/10.1371/journal.pone.0120722
- Shen YR, Wang HY, Kuo YC, et al. SEPT12 phosphorylation results in loss of the septin ring/sperm annulus, defective sperm motility and poor male fertility. PLOS Genet 2017;13: e1006631. https://doi.org/10.1371/journal.pgen.1006631
- Zhang Y, Liu G, Huang L, et al. SUN5 interacts with nuclear membrane LaminB1 and cytoskeletal GTPase Septin12 mediating the sperm head-and-tail junction. Mol Hum Reprod 2024;30:gaae022. https://doi.org/10.1093/molehr/gaae022
- Lin YH, Lin YM, Teng YN, Hsieh TYT, Lin YS, Kuo PL. Identification of ten novel genes involved in human spermatogenesis by microarray analysis of testicular tissue. Fertil Steril 2006;86:1650-8. https://doi.org/10.1016/j.fertnstert.2006.04.039
- Özkara G, Ersoy Tunali N. SEPTIN12 c.474 G>a polymorphism as a risk factor in teratozoospermic patients. Mol Biol Rep 2021;48:4073-81. https://doi.org/10.1007/s11033-021-06417-7
- Dortaj S, Gilani MAS, Sabbaghian M. Genetic investigations of SEPTIN12 gene in infertile men with acephalic sperm syndrome. Gene Rep 2025;38:102130. https://doi.org/10.1016/j.genrep.2025.102130
- Geng D, Yang X, Zhang H, et al. Association of single nucleotide polymorphism c.673C>A/p.Gln225Lys in SEPT12 gene with spermatogenesis failure in male idiopathic infertility in Northeast China. J Int Med Res 2019;47:992-8. https://doi.org/10.1177/0300060518811770
- Li Y, Wang Y, Wen Y, et al. Whole-exome sequencing of a cohort of infertile men reveals novel causative genes in teratozoospermia that are chiefly related to sperm head defects. Hum Reprod 2021;37:152-77. https://doi.org/10.1093/humrep/deab229
- Miyakawa H, Miyamoto T, Koh E, et al. Single-nucleotide polymorphisms in the SEPTIN12 gene may be a genetic risk factor for Japanese patients with Sertoli cell–only syndrome. J Androl 2012;33:483-7. https://doi.org/10.2164/jandrol.110.012146
- Chen H, Li P, Du X, et al. Homozygous loss of Septin12, but not its haploinsufficiency, leads to male infertility and fertilization failure. Front Cell Dev Biol 2022;10:850052. https://doi.org/10.3389/fcell.2022.850052
- Shen YR, Wang HY, Tsai YC, et al. The SEPT12 complex is required for the establishment of a functional sperm head–tail junction. Mol Hum Reprod 2020;26:402-12. https://doi.org/10.1093/molehr/gaaa031
- Huo JL, Zhang LQ, Zhang X, et al. Genome-wide single nucleotide polymorphism array and whole-genome sequencing reveal the inbreeding progression of Banna minipig inbred line. Anim Genet 2022;53:146-51. https://doi.org/10.1111/age.13149
- Chen HM, Xu KX, Yan C, et al. A chromosome-scale reference genome of the Banna miniature inbred pig. Sci Data 2024;11:1345. https://doi.org/10.1038/s41597-024-04201-3
- Meng J, Chen X, Wang H, Mi Y, Zhou R, Zhang H. Porcine granulosa cell transcriptomic analyses reveal the differential regulation of lncRNAs and mRNAs in response to all-trans retinoic acid in vitro. Anim Biosci 2025;38:267-77. https://doi.org/10.5713/ab.24.0363
- Chen KR, Wang HY, Kuo YC, Lo YC, Kuo PL. A novel SEPT12 mutation, T96I, is associated with sperm head and annulus defects. Front Cell Dev Biol 2025;12:1498013. https://doi.org/10.3389/fcell.2024.1498013
- Groenen MAM, Archibald AL, Uenishi H, et al. Analyses of pig genomes provide insight into porcine demography and evolution. Nature 2012;491:393-8. https://doi.org/10.1038/nature11622
- Steels JD, Estey MP, Froese CD, Reynaud D, Pace-Asciak C, Trimble WS. Sept12 is a component of the mammalian sperm tail annulus. Cell Motil Cytoskeleton 2007;64:794-807. https://doi.org/10.1002/cm.20224
- van Son M, Tremoen NH, Gaustad AH, et al. Transcriptome profiling of porcine testis tissue reveals genes related to sperm hyperactive motility. BMC Vet Res 2020;16:161. https://doi.org/10.1186/s12917-020-02373-9
- Ding X, Yu W, Liu M, et al. SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells. BMB Rep 2007;40:973-8. https://doi.org/10.5483/BMBRep.2007.40.6.973
- Lin YH, Kuo YC, Chiang HS, Kuo PL. The role of the septin family in spermiogenesis. Spermatogenesis 2011;1:298-302. https://doi.org/10.4161/spmg.1.4.18326
- Kubota T, Myung K, Donaldson AD. Is PCNA unloading the central function of the Elg1/ATAD5 replication factor C-like complex? Cell Cycle 2013;12:2570-9. https://doi.org/10.4161/cc.25626
- Park SH, Kang N, Song E, et al. ATAD5 promotes replication restart by regulating RAD51 and PCNA in response to replication stress. Nat Commun 2019;10:5718. https://doi.org/10.1038/s41467-019-13667-4
- Castillo JP, Rui H, Basilio D, et al. Mechanism of potassium ion uptake by the Na+/K+-ATPase. Nat Commun 2015;6:7622. https://doi.org/10.1038/ncomms8622
- Valdivia MM, Hamdouch K, Ortiz M, Astola A. CENPA a genomic marker for centromere activity and human diseases. Curr Genom 2009;10:326-35. https://doi.org/10.2174/138920209788920985
- Okada M, Cheeseman IM, Hori T, et al. The CENP-H–I complex is required for the efficient incorporation of newly synthesized CENP-A into centromeres. Nat Cell Biol 2006;8:446-57. https://doi.org/10.1038/ncb1396
- Laity JH, Lee BM, Wright PE. Zinc finger proteins: new insights into structural and functional diversity. Curr Opin Struct Biol 2001;11:39-46. https://doi.org/10.1016/S0959-440X(00)00167-6
- Henriques BJ, Olsen RKJ, Gomes CM, Bross P. Electron transfer flavoprotein and its role in mitochondrial energy metabolism in health and disease. Gene 2021;776:145407. https://doi.org/10.1016/j.gene.2021.145407
- Greber BJ, Ban N. Structure and function of the mitochondrial ribosome. Annu Rev Biochem 2016;85:103-32. https://doi.org/10.1146/annurev-biochem-060815-014343
- Deng S, Yang L, Gao L, Ning C, Wang S, Zhang W. The effect of combined cryoprotectants on the cryotolerance of boar sperm. Anim Biosci 2025;38:2111-24. https://doi.org/10.5713/ab.24.0915
- Urbańska K, Orzechowski A. Unappreciated role of LDHA and LDHB to control apoptosis and autophagy in tumor cells. Int J Mol Sci 2019;20:2085. https://doi.org/10.3390/ijms20092085
- Maekawa M, Ito C, Toyama Y, et al. Stage-specific expression of mouse germ cell-less-1 (mGCL-1), and multiple deformations during mgcl-1 deficient spermatogenesis leading to reduced fertility. Arch Histol Cytol 2004;67:335-47. https://doi.org/10.1679/aohc.67.335
- Adam JC, Pringle JR, Peifer M. Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization. Mol Biol Cell 2000;11:3123-35. https://doi.org/10.1091/mbc.11.9.3123
- Park C, Choi Y, Yoo S, La H, Hong K. Analysis of DNA methylation changes following Cfp1 knockout in mouse spermatocytes. Anim Biosci 2025;38:1570-9. https://doi.org/10.5713/ab.24.0807
- Mao Y, Nickitenko A, Duan X, et al. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell 2000; 100:447-56. https://doi.org/10.1016/S0092-8674(00)80680-7
- Wang L, Liu H, Zhang X, et al. WFS1 functions in ER export of vesicular cargo proteins in pancreatic β-cells. Nat Commun 2021;12:6996. https://doi.org/10.1038/s41467-021-27344-y
- Panfili E, Mondanelli G, Orabona C, et al. Novel mutations in the WFS1 gene are associated with Wolfram syndrome and systemic inflammation. Hum Mol Genet 2021;30:265-76. https://doi.org/10.1093/hmg/ddab040