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Comment
. 2011 May 19;9(5):349-50.
doi: 10.1016/j.chom.2011.05.003.

Trim5 TAKes on pattern recognition

Semih U Tareen  1 , Michael Emerman
Affiliations
Comment

Trim5 TAKes on pattern recognition

Semih U Tareen et al. Cell Host Microbe. .

Abstract

Retroviral capsids can be recognized and degraded by a host protein, Trim5α. A recent study in Nature (Pertel et al., 2011) shows that, upon sensing of the retrovirus capsid lattice, Trim5α generates free ubiquitin chains that activate the TAK1 kinase and downstream innate immune response genes.

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Figures

Figure 1
Figure 1
Trim5α functions as a PRR to activate innate immunity signaling. Upon sensing viral capsid, Trim5α, together with E2-conjugating enzymes UBC13/UEV1A, catalyzes the synthesis of K63-linked polyubiquitin (poly-Ub) chains. These chains serve as a scaffold to recruit the TAK1 kinase complex consisting of TAK1 and the regulatory proteins TAB2 and TAB3. These events result in activation of TAK1 via its auto-phosphorylation on Thr187, subsequently activating transcriptional regulators such as NF-κB. Trim5 also plays a role in LPS signaling via the Toll-like receptor 4.
See this image and copyright information in PMC

Comment on

  • TRIM5 is an innate immune sensor for the retrovirus capsid lattice.
    Pertel T, Hausmann S, Morger D, Züger S, Guerra J, Lascano J, Reinhard C, Santoni FA, Uchil PD, Chatel L, Bisiaux A, Albert ML, Strambio-De-Castillia C, Mothes W, Pizzato M, Grütter MG, Luban J. Pertel T, et al. Nature. 2011 Apr 21;472(7343):361-5. doi: 10.1038/nature09976. Nature. 2011. PMID: 21512573 Free PMC article.

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