泛素化蛋白在 TRIM30 细胞质小体中的降解作用。

Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies.

机构信息

Department of Biochemistry, College of Life Science and Technology, Yonsei University, Seoul, Republic of Korea.

Department of Integrated Omics for Biomedical Science, Yonsei University, Seoul, Republic of Korea.

出版信息

Exp Mol Med. 2015 Apr 17;47:e159. doi: 10.1038/emm.2015.12.

DOI:10.1038/emm.2015.12

PMID:25882191

Abstract

Viral infection induces numerous tripartite motif (TRIM) proteins to control antiviral immune signaling and viral replication. Particularly, SPRY-containing TRIM proteins are found only in vertebrates and they control target protein degradation by their RING-finger and SPRY domains, and proper cytoplasmic localization. To understand TRIM30 function, we analyzed its localization pattern and putative roles of its RING-finger and SPRY domains. We found that TRIM30 is located in actin-mediated cytoplasmic bodies and produces colocalized ubiquitin chains in SPRY domain- and RING-finger domain-dependent ways that are degraded by autophagy and the proteasome. These results suggest a TRIM protein-dependent degradation mechanism by cytoplasmic body formation with actin networks.

摘要

病毒感染诱导大量三肽基重复序列（TRIM）蛋白来控制抗病毒免疫信号和病毒复制。特别是，含有 SPRY 结构域的 TRIM 蛋白仅存在于脊椎动物中，它们通过其 RING 指结构域和 SPRY 结构域以及适当的细胞质定位来控制靶蛋白的降解。为了了解 TRIM30 的功能，我们分析了其定位模式及其 RING 指结构域和 SPRY 结构域的可能作用。我们发现，TRIM30 位于肌动蛋白介导的细胞质体内，并以依赖于 SPRY 结构域和 RING 指结构域的方式产生共定位的泛素链，这些泛素链通过自噬和蛋白酶体降解。这些结果表明，通过形成与肌动蛋白网络的细胞质体，存在一种依赖于 TRIM 蛋白的降解机制。