한빛사논문
- 조회1,508
Abstract
Aravinth Kumar Jayabalan1, Anthony Sanchez2, Ra Young Park1, Sang Pil Yoon3, Gum-Yong Kang4, Je-Hyun Baek4, Paul Anderson5, Younghoon Kee2 & Takbum Ohn1,*
1 Department of Cellular & Molecular Medicine, College of Medicine, Chosun University, Gwangju 61452, Republic of Korea. 2 Department of Cell Biology, Microbiology, and Molecular Biology, College of Arts and Sciences, University of South Florida, Tampa, Florida 33620, USA. 3 Department of Anatomy, School of Medicine, Jeju National University, Jeju-Do 690-756, Republic of Korea. 4 Diatech Korea Co, Ltd, Saemal-ro 5-gil, Songpa-gu, Seoul 05807, Republic of Korea. 5 Division of Rheumatology, Immunology and Allergy, Brigham and Women’s Hospital, Smith652, One Jimmy Fund Way, Boston, Massachusetts 02115, USA.
*Correspondence to : Takbum Ohn
Abstract
Stress granules (SGs) harbour translationally stalled messenger ribonucleoproteins and play important roles in regulating gene expression and cell fate. Here we show that neddylation promotes SG assembly in response to arsenite-induced oxidative stress. Inhibition or depletion of key components of the neddylation machinery concomitantly inhibits stress-induced polysome disassembly and SG assembly. Affinity purification and subsequent mass-spectrometric analysis of Nedd8-conjugated proteins from translationally stalled ribosomal fractions identified ribosomal proteins, translation factors and RNA-binding proteins (RBPs), including SRSF3, a previously known SG regulator. We show that SRSF3 is selectively neddylated at Lys85 in response to arsenite. A non-neddylatable SRSF3 (K85R) mutant do not prevent arsenite-induced polysome disassembly, but fails to support the SG assembly, suggesting that the neddylation pathway plays an important role in SG assembly.
논문정보
- Research article
- 2016년 07월 (BRIC 등록일 2016-08-03)
- 국내(교신)+국외 연구진
- 의약학 > 분자세포의학
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