Tripartite Motif Containing Protein 5 (TRIM5)

TRIM5α; TRIM5alpha; TRIM5-alpha; RNF88; RING finger protein 88

SPN	R751
HGNC	16276
MGI	2441735
PubMed	21512573
RGD	1304579
UniProt	Q9C035
Wiki	TRIM5alpha

TRIM5α belongs to the TRIM protein family; this family was first identified by Reddy in 1992 as the proteins that contain a RING finger zinc binding domain, a B-box zinc binding domain, followed by a coiled-coil region. TRIM5α bears the C-terminal PRY-SPRY or B30.2 domain in addition to the other domains. When a retrovirus enters a host cell’s cytoplasm, it undergoes processes such as capsid uncoating and reverse transcription. TRIM5 present in the cytoplasm recognizes motifs within the capsid proteins and interferes with the uncoating process, therefore preventing successful reverse transcription and transport to the nucleus of the viral genome. The exact mechanism of action has not been shown conclusively, but capsid protein from restricted viruses is removed by proteasome-dependent degradation.

Reference

"The tripartite motif family identifies cell compartments."
EMBO J. 20:2140-2151(2001) [PubMed] [Europe PMC] [Abstract]

"Trim5alpha protein restricts both HIV-1 and murine leukemia virus."
Proc. Natl. Acad. Sci. U.S.A. 101:10786-10791(2004) [PubMed] [Europe PMC] [Abstract]

"High-frequency persistence of an impaired allele of the retroviral defense gene TRIM5alpha in humans."
Curr. Biol. 16:95-100(2006) [PubMed] [Europe PMC] [Abstract]

"Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential role."
FEBS J. 275:1540-1555(2008) [PubMed] [Europe PMC] [Abstract]

"Modulation of TRIM5alpha activity in human cells by alternatively spliced TRIM5 isoforms."
J. Virol. 85:7828-7835(2011) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta."
Exp. Cell Res. 288:84-93(2003) [PubMed] [Europe PMC] [Abstract]

"Retroviral restriction factors Fv1 and TRIM5alpha act independently and can compete for incoming virus before reverse transcription."
J. Virol. 80:2100-2105(2006) [PubMed] [Europe PMC] [Abstract]

"Removal of arginine 332 allows human TRIM5alpha to bind human immunodeficiency virus capsids and to restrict infection."
J. Virol. 80:6738-6744(2006) [PubMed] [Europe PMC] [Abstract]

"Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha restriction of HIV-1."
Virology 351:112-120(2006) [PubMed] [Europe PMC] [Abstract]

"Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection."
J. Virol. 81:1054-1061(2007) [PubMed] [Europe PMC] [Abstract]

"Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]

"p62/sequestosome-1 associates with and sustains the expression of retroviral restriction factor TRIM5alpha."
J. Virol. 84:5997-6006(2010) [PubMed] [Europe PMC] [Abstract]

"Recent insights into the mechanism and consequences of TRIM5alpha retroviral restriction."
AIDS Res. Hum. Retroviruses 27:231-238(2011) [PubMed] [Europe PMC] [Abstract]

"Trim5 TAKes on pattern recognition."
Cell Host Microbe 9:349-350(2011) [PubMed] [Europe PMC] [Abstract]

"Immunology: TRIM5 does double duty."
Nature 472:305-306(2011) [PubMed] [Europe PMC] [Abstract]

"TRIM5 is an innate immune sensor for the retrovirus capsid lattice."
Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract]

"Antiviral immunity: TRIM5 moonlights as a pattern recognition receptor."
Nat. Rev. Microbiol. 9:398-398(2011) [PubMed] [Europe PMC] [Abstract]

"TRIM5alpha associates with proteasomal subunits in cells while in complex with HIV-1 virions."
Retrovirology 8:93-93(2011) [PubMed] [Europe PMC] [Abstract]

"Human Trim5alpha has additional activities that are uncoupled from retroviral capsid recognition."
Virology 409:113-120(2011) [PubMed] [Europe PMC] [Abstract]

"TRIM5 acts as more than a retroviral restriction factor."
Viruses 3:1204-1209(2011) [PubMed] [Europe PMC] [Abstract]

"TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling."
Curr. Opin. Virol. 2:142-150(2012) [PubMed] [Europe PMC] [Abstract]

"TRIM5alpha and species tropism of HIV/SIV."
Front. Microbiol. 3:13-13(2012) [PubMed] [Europe PMC] [Abstract]

"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by TRIM5alpha(rh): structure of the RING domain of TRIM5alpha."
J. Virol. 85:8725-8737(2011) [PubMed] [Europe PMC] [Abstract]

"Solution structure of the b-box domain from tripartite motif-containing protein 5."
Submitted (FEB-2009) to the PDB data bank