期刊
AUTOPHAGY
卷 15, 期 4, 页码 735-737出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2019.1569935
关键词
Arginylated substrates; autoregulation; macroautophagy; p62; ZZ domain
类别
资金
- NIH [GM106416, GM101664, GM100907, CA192642, CA218254, CA150925, CA190170]
- National Research Foundation - MSIP of Korea [NRF-2016R1A2B3011389]
- Protech Inc.
- Brain Korea 21 PLUS Program
SQSTM1/p62 facilitates responses to various cellular stresses and has been implicated in human diseases. This protein functions as a major cytoplasmic signaling hub and has multiple binding partners, including arginylated (Nt-R) proteins that are recognized by the ZZ domain of SQSTM1/p62 (SQSTM1/p62(ZZ)). We have determined the molecular mechanism of Nt-R recognition using a combination of biochemical and NMR approaches and obtained the crystal structure of SQSTM1/p62(ZZ) in complex with Nt-R. We found that binding of SQSTM1/p62(ZZ) to Nt-R induces SQSTM1/p62 puncta formation and macroautophagy/autophagy and identified a regulatory linker (RL) region of SQSTM1/p62 that associates with SQSTM1/p62(ZZ) in vitro. Our findings suggest a mechanism for SQSTM1/p62 autoregulation that can be essential in mediating autophagy.
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