한빛사논문
- 조회495
Hyun-Jun Choi1,2, Ji Young Lee3,4 and Kiyoung Kim4
1Soonchunhyang Institute of Medi-bio Science, Soonchunhyang University, Cheonan 31151, Korea.
2Department of Integrated Biomedical Sciences, Soonchunhyang University, Cheonan 31151, Korea.
3Department of Medical Biotechnology, Soonchunhyang University, Asan 31538, Korea.
4Department of Medical Science, Soonchunhyang University, Asan 31538, Korea.
Corresponding author : Correspondence to Kiyoung Kim.
Abstract
RNA-binding proteins (RBPs) containing low-sequence complexity domains mediate the formation of cellular condensates and membrane-less organelles with biological functions via liquid‒liquid phase separation (LLPS). However, the abnormal phase transition of these proteins induces the formation of insoluble aggregates. Aggregates are pathological hallmarks of neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS). The molecular mechanisms underlying aggregate formation by ALS-associated RPBs remain largely unknown. This review highlights emerging studies on various posttranslational modifications (PTMs) related to protein aggregation. We begin with the introduction of several ALS-associated RBPs that form aggregates induced by phase separation. In addition, we highlight our recent discovery of a new PTM involved in the phase transition during the pathogenesis of fused-in-sarcoma (FUS)-associated ALS. We suggest a molecular mechanism through which LLPS mediates glutathionylation in FUS-linked ALS. This review aims to provide a detailed overview of the key molecular mechanisms of LLPS-mediated aggregate formation by PTMs, which will help further the understanding of the pathogenesis and development of ALS therapeutics.
논문정보
- Review Paper
- 2023년 04월 (BRIC 등록일 2023-04-03)
- 국내 연구진
- 생명과학 > 분자생물학
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