Disruption of RNA-binding proteins in neurological disorders

被引:0
作者
Huang, Luyang [1 ]
Zhao, Bo [1 ]
Wan, Youzhong [1 ]
机构
[1] Jilin Univ, Canc Biol Lab, China Japan Union Hosp, Changchun 130062, Jilin, Peoples R China
关键词
RBPs; Neurological diseases; RNA regulation; RBP aggregation; Ectopic expression; SPINAL MUSCULAR-ATROPHY; AMYOTROPHIC-LATERAL-SCLEROSIS; PRION-LIKE DOMAINS; FRAGILE-X-SYNDROME; C-TERMINAL DOMAIN; STRESS GRANULE; PHASE-SEPARATION; MESSENGER-RNAS; NUCLEAR-IMPORT; REPEAT EXPANSION;
D O I
10.1016/j.expneurol.2024.115119
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
RNA-binding proteins (RBPs) are multifunctional proteins essential for the regulation of RNA processing and metabolism, contributing to the maintenance of cell homeostasis by modulating the expression of target genes. Many RBPs have been associated with neuron-specific processes vital for neuronal development and survival. RBP dysfunction may result in aberrations in RNA processing, which subsequently initiate a cascade of effects. Notably, RBPs are involved in the onset and progression of neurological disorders via diverse mechanisms. Disruption of RBPs not only affects RNA processing, but also promotes the abnormal aggregation of proteins into toxic inclusion bodies, and contributes to immune responses that drive the progression of neurological diseases. In this review, we summarize recent discoveries relating to the roles of RBPs in neurological diseases, discuss their contributions to such conditions, and highlight the unique functions of these RBPs within the nervous system.
引用
收藏
页数:14
相关论文
共 218 条
  • [1] Human QKI, a potential regulator of mRNA expression of human oligodendrocyte-related genes involved in schizophrenia
    Aberg, Karolina
    Saetre, Peter
    Jareborg, Niclas
    Jazin, Elena
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (19) : 7482 - 7487
  • [2] The RNA-binding protein HuD regulates neuronal cell identity and maturation
    Akamatsu, W
    Fujihara, H
    Mitsuhashi, T
    Yano, M
    Shibata, S
    Hayakawa, Y
    Okano, HJ
    Sakakibara, S
    Takano, H
    Takano, T
    Takahashi, T
    Noda, T
    Okano, H
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (12) : 4625 - 4630
  • [3] Andersen JS, 2002, CURR BIOL, V12, P1, DOI 10.1016/S0960-9822(01)00650-9
  • [4] Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo
    Apicco, Daniel J.
    Ash, Peter E. A.
    Maziuk, Brandon
    LeBlang, Chelsey
    Medalla, Maria
    Al Abdullatif, Ali
    Ferragud, Antonio
    Botelho, Emily
    Ballance, Heather I.
    Dhawan, Uma
    Boudeau, Samantha
    Cruz, Anna Lourdes
    Kashy, Daniel
    Wong, Aria
    Goldberg, Lisa R.
    Yazdani, Neema
    Zhang, Cheng
    Ung, Choong Y.
    Tripodis, Yorghos
    Kanaan, Nicholas M.
    Ikezu, Tsuneya
    Cottone, Pietro
    Leszyk, John
    Li, Hu
    Luebke, Jennifer
    Bryant, Camron D.
    Wolozin, Benjamin
    [J]. NATURE NEUROSCIENCE, 2018, 21 (01) : 72 - +
  • [5] TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    Arai, Tetsuaki
    Hasegawa, Masato
    Akiyama, Haruhiko
    Ikeda, Kenji
    Nonaka, Takashi
    Mori, Hiroshi
    Mann, David
    Tsuchiya, Kuniaki
    Yoshida, Marl
    Hashizume, Yoshio
    Oda, Tatsuro
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2006, 351 (03) : 602 - 611
  • [6] TIA1 oxidation inhibits stress granule assembly and sensitizes cells to stress-induced apoptosis
    Arimoto-Matsuzaki, Kyoko
    Saito, Haruo
    Takekawa, Mutsuhiro
    [J]. NATURE COMMUNICATIONS, 2016, 7
  • [7] Mouse Ataxin-2 Expansion Downregulates CamKII and Other Calcium Signaling Factors, Impairing Granule-Purkinje Neuron Synaptic Strength
    Arsovic, Aleksandar
    Halbach, Melanie Vanessa
    Canet-Pons, Julia
    Esen-Sehir, Dilhan
    Doering, Claudia
    Freudenberg, Florian
    Czechowska, Nicoletta
    Seidel, Kay
    Baader, Stephan L.
    Gispert, Suzana
    Sen, Nesli-Ece
    Auburger, Georg
    [J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2020, 21 (18) : 1 - 36
  • [8] Restoring SMN Expression: An Overview of the Therapeutic Developments for the Treatment of Spinal Muscular Atrophy
    Aslesh, Tejal
    Yokota, Toshifumi
    [J]. CELLS, 2022, 11 (03)
  • [9] Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP
    Aulas, Anais
    Stabile, Stephanie
    Velde, Christine Vande
    [J]. MOLECULAR NEURODEGENERATION, 2012, 7
  • [10] Structural determinants of the cellular localization and shuttling of TDP-43
    Ayala, Youhna M.
    Zago, Paola
    D'Ambrogio, Andrea
    Xu, Ya-Fei
    Petrucelli, Leonard
    Buratti, Emanuele
    Baralle, Francisco E.
    [J]. JOURNAL OF CELL SCIENCE, 2008, 121 (22) : 3778 - 3785