Heterogeneous Nuclear Ribonucleoprotein in Regulating Oocyte Development

doi:10.12280/gjszjk.20250343

Abstract

Abstract:

The family of heterogeneous nuclear ribonucleoprotein (hnRNP) includes more than twenty kinds of RNA-binding proteins that play an important role in many life processes. Besides RNA binding, hnRNP mainly involved in regulating key biological processes such as N6-methyladenosine (m⁶A) modification and DNA damage repair. Many studies have shown that many members of hnRNP family, including HNRNPA2B1, HNRNPC, HNRNPH1 and HNRNPK, play an important role in the development of oocytes, and that the loss of hnRNP function can lead to the abnormal development of oocytes and infertility. However, the in-depth mechanism reaserch of hnRNP regulating oocyte development is insufficient. Reviewing the biological function of hnRNP in regulating oocyte development can provide reference for future research in reproductive field.

Key words: Heterogeneous-nuclear ribonucleoproteins, RNA-binding proteins, Oogenesis, Reproduction, Methylation

XIAO Jin-xin, XIONG Meng-neng, XIE Qing-zhen. Heterogeneous Nuclear Ribonucleoprotein in Regulating Oocyte Development[J]. Journal of International Reproductive Health/Family Planning, 2025, 44(6): 486-489.

References 33

[1]	Piñol-Roma S, Choi YD, Matunis MJ, et al. Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins[J]. Genes Dev, 1988, 2(2):215-227. doi: 10.1101/gad.2.2.215.
[2]	Dreyfuss G. RNA-binding proteins in disease etiology: fragile X syndrome and spinal muscular atrophy[J]. RNA, 2025, 31(3):277-283. doi: 10.1261/rna.080353.124. pmid: 39694825
[3]	Balasubramanian S, Roy I, Appadurai R, et al. The ribonucleoprotein hnRNPA1 mediates binding to RNA and DNA telomeric G-quadruplexes through an RGG-rich region[J]. J Biol Chem, 2025, 301(5):108491. doi: 10.1016/j.jbc.2025.108491.
[4]	Liu Y, Abula A, Xiao H, et al. Structural Insight Into hnRNP A2/B1 Homodimerization and DNA Recognition[J]. J Mol Biol, 2023, 435(3):167920. doi: 10.1016/j.jmb.2022.167920.
[5]	Zhang Z, Wu T, Sang Q, et al. Human oocyte quality and reproductive health[J]. Sci Bull(Beijing), 2025, 70(14):2365-2376. doi: 10.1016/j.scib.2025.04.045.
[6]	Ducreux B, Ferreux L, Patrat C, et al. Overview of Gene Expression Dynamics during Human Oogenesis/Folliculogenesis[J]. Int J Mol Sci, 2023, 25(1):33. doi: 10.3390/ijms25010033.
[7]	Liu Y, Sun Z, Gui D, et al. RNA Modification in Metabolism[J]. MedComm (2020),2025, 6(3):e70135. doi: 10.1002/mco2.70135.
[8]	Qiu L, Wu S, Zhang L, et al. The biological roles and molecular mechanisms of m⁶A reader IGF2BP1 in the hallmarks of cancer[J]. Genes Dis, 2025, 12(5):101567.doi: 10.1016/j.gendis.2025.101567.
[9]	Teng H, Stoiber M, Bar-Joseph Z, et al. Detecting m⁶A RNA modification from nanopore sequencing using a semisupervised learning framework[J]. Genome Res, 2024, 34(11):1987-1999. doi: 10.1101/gr.278960.124.
[10]	Xiang Y, Chang HM, Leung P, et al. RNA modifications in female reproductive physiology and disease: emerging roles and clinical implications[J]. Hum Reprod Update, 2025, 31(4):333-360. doi: 10.1093/humupd/dmaf005.
[11]	Li P, Lin Y, Ma H, et al. Epigenetic regulation in female reproduction: the impact of m6A on maternal-fetal health[J]. Cell Death Discov, 2025, 11(1):43. doi: 10.1038/s41420-025-02324-z. pmid: 39904996
[12]	Alarcón CR, Goodarzi H, Lee H, et al. HNRNPA2B1 Is a Mediator of m⁶A-Dependent Nuclear RNA Processing Events[J]. Cell, 2015, 162(6):1299-1308. doi: 10.1016/j.cell.2015.08.011.
[13]	Liu N, Dai Q, Zheng G, et al. N⁶-methyladenosine-dependent RNA structural switches regulate RNA-protein interactions[J]. Nature, 2015, 518(7540):560-564. doi: 10.1038/nature14234.
[14]	Liu N, Zhou KI, Parisien M, et al. N6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein[J]. Nucleic Acids Res, 2017, 45(10):6051-6063. doi: 10.1093/nar/gkx141. pmid: 28334903
[15]	Kumar A, Daripa P, Penumutchu S, et al. Thermodynamic insights into N6-methyladenosine-modified ribonucleic acids and their interactions with the RNA recognition motif of heterogeneous nuclear ribonucleoprotein C[J]. Int J Biol Macromol, 2025,312:144210. doi: 10.1016/j.ijbiomac.2025.144210.
[16]	Ivanova I, Much C, Di Giacomo M, et al. The RNA m⁶A Reader YTHDF2 Is Essential for the Post-transcriptional Regulation of the Maternal Transcriptome and Oocyte Competence[J]. Mol Cell, 2017, 67(6):1059-1067.e4. doi: 10.1016/j.molcel.2017.08.003. pmid: 28867294
[17]	Das BB, Basu S, Sengupta A, et al. Post-Translational Modifications Orchestrate Repair of Trapped Topoisomerase-Induced DNA Breaks via TDP1 and TDP2[J]. J Mol Biol, 2025:169309. doi: 10.1016/j.jmb.2025.169309.
[18]	Nesic K, Parker P, Swisher EM, et al. DNA repair and the contribution to chemotherapy resistance[J]. Genome Med, 2025, 17(1):62. doi: 10.1186/s13073-025-01488-8.
[19]	Alfano L, Caporaso A, Altieri A, et al. Depletion of the RNA binding protein HNRNPD impairs homologous recombination by inhibiting DNA-end resection and inducing R-loop accumulation[J]. Nucleic Acids Res, 2019, 47(8):4068-4085. doi: 10.1093/nar/gkz076. pmid: 30799487
[20]	Wang Z, Qu M, Chang S, et al. Human RNA-binding protein HNRNPD interacts with and regulates the repair of deoxyribouridine in DNA[J]. Int J Biol Macromol, 2024, 262(Pt 1):129951. doi: 10.1016/j.ijbiomac.2024.129951.
[21]	Refaat AM, Nakata M, Husain A, et al. HNRNPU facilitates antibody class-switch recombination through C-NHEJ promotion and R-loop suppression[J]. Cell Rep, 2023, 42(3):112284. doi: 10.1016/j.celrep.2023.112284.
[22]	Morales-Sánchez E, Campuzano-Caballero JC, Cervantes A, et al. Which Side of the Coin Are You on Regarding Possible Postnatal Oogenesis?[J]. Arch Med Res, 2024, 55(8):103071. doi: 10.1016/j.arcmed.2024.103071.
[23]	Ma Y, Hong Y, Gao R, et al. Maternal exposure to Aristolochic Acid I affects meiotic I progression by impairing DNA damage repair in fetal oocytes[J]. Ecotoxicol Environ Saf, 2025,295:118137. doi: 10.1016/j.ecoenv.2025.118137.
[24]	Lee PC, Wildt DE, Comizzoli P. Proteomic analysis of germinal vesicles in the domestic cat model reveals candidate nuclear proteins involved in oocyte competence acquisition[J]. Mol Hum Reprod, 2018, 24(1):14-26. doi: 10.1093/molehr/gax059. pmid: 29126204
[25]	Wu ZW, Mou Q, Fang T, et al. Global 3′-untranslated region landscape mediated by alternative polyadenylation during meiotic maturation of pig oocytes[J]. Reprod Domest Anim, 2022, 57(1):33-44. doi: 10.1111/rda.14026.
[26]	Zhou CX, Wang SQ, Zhang JY, et al. HNRNPA2B1-mediated m6A modification enhances lncRNA NORHA stability to control granulosa cell functions[J]. Zool Res, 2025, 46(3):722-732. doi: 10.24272/j.issn.2095-8137.2024.378.
[27]	Zhu S, Hou J, Gao H, et al. SUMOylation of HNRNPA2B1 modulates RPA dynamics during unperturbed replication and genotoxic stress responses[J]. Mol Cell, 2023, 83(4):539-555.e7. doi: 10.1016/j.molcel.2023.01.003. pmid: 36702126
[28]	Chen F, Xu W, Tang M, et al. hnRNPA2B1 deacetylation by SIRT6 restrains local transcription and safeguards genome stability[J]. Cell Death Differ, 2025, 32(3):382-396. doi: 10.1038/s41418-024-01412-4. pmid: 39511404
[29]	Xiong X, Feng S, Ma X, et al. hnRNPC Functions with HuR to Regulate Alternative Splicing in an m6A-Dependent Manner and is Essential for Meiosis[J]. Adv Sci (Weinh), 2025, 12(13):e2412196. doi: 10.1002/advs.202412196.
[30]	Sun D, Wang Y, Sun N, et al. LncRNA DANCR counteracts premature ovarian insufficiency by regulating the senescence process of granulosa cells through stabilizing the interaction between p53 and hNRNPC[J]. J Ovarian Res, 2023, 16(1):41. doi: 10.1186/s13048-023-01115-3. pmid: 36805799
[31]	Feng S, Wen H, Liu K, et al. hnRNPH1 establishes Sertoli-germ cell crosstalk through cooperation with PTBP1 and AR, and is essential for male fertility in mice[J]. Development, 2023, 150(3):dev201040. doi: 10.1242/dev.201040.
[32]	Wang N, Zhang P, Guo X, et al. Hnrnpk, a protein differentially expressed in immature rat ovarian development, is required for normal primordial follicle assembly and development[J]. Endocrinology, 2011, 152(3):1024-1035. doi: 10.1210/en.2010-0797. pmid: 21190960
[33]	Zhang P, Wang N, Lin X, et al. Expression and localization of heterogeneous nuclear ribonucleoprotein K in mouse ovaries and preimplantation embryos[J]. Biochem Biophys Res Commun, 2016, 471(1):260-265. doi: 10.1016/j.bbrc.2016.02.003.