TRIM22 E3 ubiquitin ligase activity is required to mediate antiviral activity against encephalomyocarditis virus
نویسندگان
چکیده
منابع مشابه
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
PINK1 kinase activates the E3 ubiquitin ligase Parkin to induce selective autophagy of damaged mitochondria. However, it has been unclear how PINK1 activates and recruits Parkin to mitochondria. Although PINK1 phosphorylates Parkin, other PINK1 substrates appear to activate Parkin, as the mutation of all serine and threonine residues conserved between Drosophila and human, including Parkin S65,...
متن کاملDual-site regulation of MDM2 E3-ubiquitin ligase activity.
The control of p53 ubiquitination by MDM2 provides a model system to define how an E3-ligase functions on a conformationally flexible substrate. The mechanism of MDM2-mediated ubiquitination of p53 has been analyzed by deconstructing, in vitro, the MDM2-dependent ubiquitination reaction. Surprisingly, ligands binding to the hydrophobic cleft of MDM2 do not inhibit its E3-ligase function. Howeve...
متن کاملAntiviral activity of bacteria-derived human alpha interferons against encephalomyocarditis virus infection of mice.
Bacteria-derived human leukocyte interferon (IFN) subtypes, IFN-alpha A, -alpha B, and -alpha D, and two hybrid IFNs, IFN-alpha AD and -alpha DA, were examined for both in vitro and in vivo antiviral activity. Two of these materials in highly purified form (IFN-alpha D and -alpha D) protect mice against lethal doses of encephalomyocarditis virus infection. A single dose of 1 microgram of protei...
متن کاملE3 Ubiquitin Ligase NEDD4 Promotes Influenza Virus Infection by Decreasing Levels of the Antiviral Protein IFITM3
Interferon (IFN)-induced transmembrane protein 3 (IFITM3) is a cell-intrinsic factor that limits influenza virus infections. We previously showed that IFITM3 degradation is increased by its ubiquitination, though the ubiquitin ligase responsible for this modification remained elusive. Here, we demonstrate that the E3 ubiquitin ligase NEDD4 ubiquitinates IFITM3 in cells and in vitro. This IFITM3...
متن کاملThe E3 ubiquitin ligase activity of RING1B is not essential for early mouse development.
Polycomb-repressive complex 1 (PRC1) and PRC2 maintain repression at many developmental genes in mouse embryonic stem cells and are required for early development. However, it is still unclear how they are targeted and how they function. We show that the ability of RING1B, a core component of PRC1, to ubiquitinate histone H2A is dispensable for early mouse embryonic development and much of the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of General Virology
سال: 2009
ISSN: 0022-1317,1465-2099
DOI: 10.1099/vir.0.006288-0