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Literature summary for 2.3.2.26 extracted from

  • Zhu, B.; Das, S.; Mitra, S.; Farris, T.; McBride, J.
    Ehrlichia chaffeensis TRP120 moonlights as a HECT E3 ligase involved in selfand host ubiquitination to influence protein interactions and stability for intracellular survival (2017), Infect. Immun., 85, e00290 .
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Ehrlichia chaffeensis
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-
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Homo sapiens Q96PU5
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
ubiquitination TRP120 is posttranslationally modified by ubiquitin. Ubiquitination occurs through intrinsic and host-mediated HECT ligase activity Ehrlichia chaffeensis

Synonyms

Synonyms Comment Organism
Trp120
-
 Ehrlichia chaffeensis

General Information

General Information Comment Organism
physiological function Ehrlichia chaffeensis tandem repeat protein TRP120 is posttranslationally modified by ubiquitin. Ubiquitination occurs through intrinsic and host-mediated HECT ligase activity. HECT E3 ubiquitin ligase, Nedd4L, interacts with TRP120 during infection and also mediates TRP120 ubiquitination. Nedd4L knockdown results in the reduction of TRP120 ubiquitination, decreases ehrlichial infection, and reduces recruitment of TRP120-interacting host protein, PCGF5, to ehrlichial inclusions. TRP120-mediated PCGF5 polyubiquitination is associated with a reduction in PCGF5 levels. Inhibition of ubiquitination with small molecules also significantly decreases ehrlichial infection Homo sapiens
physiological function Ehrlichia chaffeensis tandem repeat protein TRP120 is posttranslationally modified by ubiquitin. Ubiquitination occurs through intrinsic and host-mediated HECT ligase activity. The C-terminal region of TRP120 harbors a functional HECT E3 ligase domain with a conserved catalytic site. TRP120 autoubiquitination occurs in vitro in the presence of host UbcH5b/c E2 enzymes. Human HECT E3 ubiquitin ligase, Nedd4L, interacts with TRP120 during infection and also mediates TRP120 ubiquitination. Nedd4L knockdown results in the reduction of TRP120 ubiquitination, decreases ehrlichial infection, and reduces recruitment of TRP120-interacting host protein, PCGF5, to ehrlichial inclusions. TRP120-mediated PCGF5 polyubiquitination is associated with a reduction in PCGF5 levels. Inhibition of ubiquitination with small molecules also significantly decreases ehrlichial infection Ehrlichia chaffeensis