B30.2/SPRY domain in tripartite motif-containing 22 is essential for the formation of distinct nuclear bodies

被引：20

作者：

Sivaramakrishnan, Gayathri ^{[1
]}

Sun, Yang ^{[1
]}

Rajmohan, Rajamuthiah ^{[1
]}

Lin, Valerie C. L. ^{[1
]}

机构：

[1] Nanyang Technol Univ, Sch Biol Sci, Singapore 637551, Singapore

来源：

FEBS LETTERS | 2009年 / 583卷 / 12期

关键词：

Tripartite motif-containing 22; B30.2/SplA and ryanodine receptor; Nuclear body; Nuclear localization; ACUTE PROMYELOCYTIC LEUKEMIA; E3 UBIQUITIN LIGASE; SYNDROME GENE-PRODUCT; RING FINGER DOMAIN; OPITZ-SYNDROME; PML BODIES; CELL-CYCLE; PROTEIN; TRIM5-ALPHA; GROWTH;

D O I：

10.1016/j.febslet.2009.05.036

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tripartite motif-containing 22 (TRIM22) is an important antiviral protein that forms distinct nuclear bodies (NB) in many cell types. This study aims to identify functional domains/residues for TRIM22's nuclear localization and NB formation. Deletion of the really-interesting-new-gene (RING) domain, which is essential for its antiviral property, abolished TRIM22 NB formation. However, mutation of two critical residues Cys15 and Cys18 to alanine in the RING domain, did not affect NB formation notably. Although the deletion of the putative bipartite nuclear localization signal (NLS) abolished TRIM22 localization and NB formation, the B30.2/SplA and ryanodine receptor (SPRY) domain, and residues 491-494 specifically are also essential for nuclear localization and NB formation. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：2093 / 2099

页数：7

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