New insights into the role of the Golgi apparatus in the pathogenesis and therapeutics of human diseases

被引:14
作者
Choi, Wooseon [1 ]
Kang, Shinwon [2 ,3 ]
Kim, Jiyoon [1 ]
机构
[1] Catholic Univ Korea, Coll Med, Dept Biomed & Hlth Sci, Dept Pharmacol, Seoul 06591, South Korea
[2] Univ Toronto, Dept Physiol, Toronto, ON, Canada
[3] Sinai Hlth Syst, Mt Sinai Hosp, Lunenfeld Tanenbaum Res Inst, Toronto, ON, Canada
基金
新加坡国家研究基金会;
关键词
Golgi apparatus; Human disease; Pathogenesis; Therapeutic target; AMYOTROPHIC-LATERAL-SCLEROSIS; LONG-TERM POTENTIATION; CASPASE-MEDIATED CLEAVAGE; ALZHEIMERS-DISEASE; STRESS-RESPONSE; MOTOR-NEURONS; UNCONVENTIONAL SECRETION; ENDOPLASMIC-RETICULUM; TRANSCRIPTION FACTORS; FRAGMENTATION;
D O I
10.1007/s12272-022-01408-z
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
The Golgi apparatus is an essential cellular organelle that mediates homeostatic functions, including vesicle trafficking and the post-translational modification of macromolecules. Its unique stacked structure and dynamic functions are tightly regulated, and several Golgi proteins play key roles in the functioning of unconventional protein secretory pathways triggered by cellular stress responses. Recently, an increasing number of studies have implicated defects in Golgi functioning in human diseases such as cancer, neurodegenerative, and immunological disorders. Understanding the extraordinary characteristics of Golgi proteins is important for elucidating its associated intracellular signaling mechanisms and has important ramifications for human health. Therefore, analyzing the mechanisms by which the Golgi participates in disease pathogenesis may be useful for developing novel therapeutic strategies. This review articulates the structural features and abnormalities of the Golgi apparatus reported in various diseases and the suspected mechanisms underlying the Golgi-associated pathologies. Furthermore, we review the potential therapeutic strategies based on Golgi function.
引用
收藏
页码:671 / 692
页数:22
相关论文
共 236 条
[41]   TMEM165 deficiencies in Congenital Disorders of Glycosylation type II(CDG-II): Clues and evidences for roles of the protein in Golgi functions and ion homeostasis [J].
Dulary, Eudoxie ;
Potelle, Sven ;
Legrand, Dominique ;
Foulquier, Francois .
TISSUE & CELL, 2017, 49 (02) :150-156
[42]   Autophagy-based unconventional secretory pathway for extracellular delivery of IL-1β [J].
Dupont, Nicolas ;
Jiang, Shanya ;
Pilli, Manohar ;
Ornatowski, Wojciech ;
Bhattacharya, Dhruva ;
Deretic, Vojo .
EMBO JOURNAL, 2011, 30 (23) :4701-4711
[43]   A Novel RAB33B Mutation in SmithMcCort Dysplasia [J].
Dupuis, Nina ;
Lebon, Sophie ;
Kumar, Manoj ;
Drunat, Severine ;
Graul-Neumann, Luitgard M. ;
Gressens, Pierre ;
El Ghouzzi, Vincent .
HUMAN MUTATION, 2013, 34 (02) :283-286
[44]   Golgi organization is regulated by proteasomal degradation [J].
Eisenberg-Lerner, Avital ;
Benyair, Ron ;
Hizkiahou, Noa ;
Nudel, Neta ;
Maor, Roey ;
Kramer, Matthias P. ;
Shmueli, Merav D. ;
Zigdon, Inbal ;
Lev, Marina Cherniavsky ;
Ulman, Adi ;
Sagiv, Jitka Yehudith ;
Dayan, Molly ;
Dassa, Bareket ;
Rosenwald, Mercedes ;
Shachar, Idit ;
Li, Jie ;
Wang, Yanzhuang ;
Dezorella, Nili ;
Khan, Suman ;
Porat, Ziv ;
Shimoni, Eyal ;
Avinoam, Ori ;
Merbl, Yifat .
NATURE COMMUNICATIONS, 2020, 11 (01)
[45]   S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi [J].
Ernst, Andreas M. ;
Syed, Saad A. ;
Zaki, Omar ;
Bottanelli, Francesca ;
Zheng, Hong ;
Hacke, Moritz ;
Xi, Zhiqun ;
Rivera-Molina, Felix ;
Graham, Morven ;
Rebane, Aleksander A. ;
Bjorkholm, Patrik ;
Baddeley, David ;
Toomre, Derek ;
Pincet, Frederic ;
Rothman, James E. .
DEVELOPMENTAL CELL, 2018, 47 (04) :479-+
[46]   Advances in understanding N-glycosylation structure, function, and regulation in health and disease [J].
Esmail, Sally ;
Manolson, Morris F. .
EUROPEAN JOURNAL OF CELL BIOLOGY, 2021, 100 (7-8)
[47]   DNA Damage Triggers Golgi Dispersal via DNA-PK and GOLPH3 [J].
Farber-Katz, Suzette E. ;
Dippold, Holly C. ;
Buschman, Matthew D. ;
Peterman, Marshall C. ;
Xing, Mengke ;
Noakes, Christopher J. ;
Tat, John ;
Ng, Michelle M. ;
Rahajeng, Juliati ;
Cowan, David M. ;
Fuchs, Greg J. ;
Zhou, Huilin ;
Field, Seth J. .
CELL, 2014, 156 (03) :413-427
[48]   EGAD! There is an ERAD doppelganger in the Golgi [J].
Fonseca, Daniel ;
Carvalho, Pedro .
EMBO JOURNAL, 2019, 38 (15)
[49]   TMEM165 Deficiency Causes a Congenital Disorder of Glycosylation [J].
Foulquier, Francois ;
Amyere, Mustapha ;
Jaeken, Jaak ;
Zeevaert, Renate ;
Schollen, Els ;
Race, Valerie ;
Bammens, Riet ;
Morelle, Willy ;
Rosnoblet, Claire ;
Legrand, Dominique ;
Demaegd, Didier ;
Buist, Neil ;
Cheillan, David ;
Guffon, Nathalie ;
Morsomme, Pierre ;
Annaert, Willem ;
Freeze, Hudson H. ;
Van Schaftingen, Emile ;
Vikkula, Miikka ;
Matthijs, Gert .
AMERICAN JOURNAL OF HUMAN GENETICS, 2012, 91 (01) :15-26
[50]   Segregation of the membrane cargoes, BACE1 and amyloid precursor protein (APP) throughout the Golgi apparatus [J].
Fourriere, Lou ;
Cho, Ellie Hyun-Jung ;
Gleeson, Paul A. .
TRAFFIC, 2022, 23 (03) :158-173