TRIM5

tripartite motif containing 5

TRIM5 is a member of a broad family of otherwise unrelated proteins defined by the presence of a tripartite motif containing a RING domain, a B-box type 1, and a B-box type 2, followed by a coiled-coil region. TRIM5 has six alternately spliced isoforms, the longest of which is the a variant which also contains a carboxy-terminal B30.2 (SPRY) domain (1). Expression of TRIM5a variants from humans, rhesus monkeys, and African green monkeys enabled resistance to infection by various retroviruses including HIV-1 (2,3), albeit at differing efficiencies. All TRIM5a variants could inhibit at least two different retroviruses, but not from those viruses isolated from the same species, suggesting that TRIM5a acts as a natural barrier to cross-species retrovirus transmission (3). While a function has not yet been assigned to TRIM5g, it is known that expression of TRIM5a variants from humans, rhesus monkeys, and African green monkeys enable resistance to infection by various retroviruses including HIV-1, albeit at differing efficiencies. Furthermore, the TRIM5d isoform appears to serve as a scaffold for the assembly of endogenous BTBD1 and BTBD2 proteins and also exhibits autoubiquitination activity in a RING finger- and UbcH5B-dependent manner. The TRIM5d isoform has been shown to colocalize with the topoisomerase I-interacting proteins BTBD1 and BTBD2 in punctate or elongated cytoplasmic bodies in several mouse and human cells where it appears to serve as a scaffold for the assembly of endogenous BTBD proteins. TRIM5d also exhibits autoubiquitination activity in a RING finger- and UbcH5B-dependent manner.

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