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Trafficking of some old world primate TRIM5α proteins through the nucleus. | LitMetric

AI Article Synopsis

  • TRIM5α and TRIMCyp are proteins that play a role in preventing retroviral infections by binding to viral capsids and forming dynamic cytoplasmic structures.
  • Researchers found that TRIM5α proteins from humans and rhesus monkeys can move between the cytoplasm and the nucleus, influenced by treatment with leptomycin B.
  • This new discovery suggests that the ability of TRIM5α to shuttle into the nucleus may have a significant, yet-to-be-understood function in viral restriction.

Article Abstract

Background: TRIM5α and TRIMCyp are cytoplasmic proteins that bind incoming retroviral capsids and mediate early blocks to viral infection. TRIM5 proteins form cytoplasmic bodies, which are highly dynamic structures. So far, TRIM5 proteins have been found only in the cytoplasm of cells. Interestingly, other proteins from the TRIM family localize to the nucleus. Therefore, we tested the possibility that TRIM5 proteins traffic to the nucleus and the impact of this trafficking on retroviral restriction.

Results: Here we report that the TRIM5α proteins of two Old World primates, humans and rhesus monkeys, are transported into the nucleus and are shuttled back to the cytoplasm by a leptomycin B-sensitive mechanism. In leptomycin B-treated cells, these TRIM5α proteins formed nuclear bodies that also contained TRIM19 (PML). Deletion of the amino terminus, including the linker 1 (L1) region, resulted in TRIM5α proteins that accumulated in nuclear bodies. Leptomycin B treatment of TRIM5α-expressing target cells only minimally affected the restriction of retrovirus infection.

Conclusions: We discovered the ability of human and rhesus TRIM5α to shuttle into and out of the nucleus. This novel trafficking ability of TRIM5α proteins could be important for an as-yet-unknown function of TRIM5α.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3120760PMC
http://dx.doi.org/10.1186/1742-4690-8-38DOI Listing

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