Journal
FEBS LETTERS
Volume 583, Issue 12, Pages 2093-2099Publisher
WILEY
DOI: 10.1016/j.febslet.2009.05.036
Keywords
Tripartite motif-containing 22; B30.2/SplA and ryanodine receptor; Nuclear body; Nuclear localization
Funding
- Ministry of Education, the Republic of Singapore
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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.
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