TRIM22: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Bot: HTTP→HTTPS)
 
imported>GreenC bot
 
Line 4: Line 4:
== Function ==
== Function ==


The protein encoded by this gene is a member of the [[tripartite motif family|tripartite motif]] (TRIM) family.<ref name="pmid11331580">{{cite journal | vauthors = Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A | title = The tripartite motif family identifies cell compartments | journal = EMBO J. | volume = 20 | issue = 9 | pages = 2140–51 |date=May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 | url = | issn = | accessdate = 2009-02-22}}</ref> The TRIM motif includes three zinc-binding domains, a [[RING finger domain|RING]], a B-box type 1 and a B-box type 2, and a [[coiled coil|coiled-coil region]]. This protein localizes to the [[cytoplasm]] and its expression is induced by [[interferon]].<ref name="entrez" /> TRIM22 is also a target gene of the  [[tumor suppressor gene|tumor suppressor]] protein [[p53]].<ref name="pmid17970695">{{cite journal | vauthors = Obad S, Olofsson T, Mechti N, Gullberg U, Drott K | title = Regulation of the interferon-inducible p53 target gene TRIM22 (Staf50) in human T lymphocyte activation | journal = J. Interferon Cytokine Res. | volume = 27 | issue = 10 | pages = 857–64 |date=October 2007 | pmid = 17970695 | doi = 10.1089/jir.2006.0180 | url = http://luur.lub.lu.se/luur?func=downloadFile&fileOId=548138 | issn = }}</ref>
The protein encoded by this gene is a member of the [[tripartite motif family|tripartite motif]] (TRIM) family.<ref name="pmid11331580">{{cite journal | vauthors = Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A | title = The tripartite motif family identifies cell compartments | journal = EMBO J. | volume = 20 | issue = 9 | pages = 2140–51 |date=May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 | url = | issn = }}</ref> The TRIM motif includes three zinc-binding domains, a [[RING finger domain|RING]], a B-box type 1 and a B-box type 2, and a [[coiled coil|coiled-coil region]]. This protein localizes to the [[cytoplasm]] and its expression is induced by [[interferon]].<ref name="entrez" /> TRIM22 is also a target gene of the  [[tumor suppressor gene|tumor suppressor]] protein [[p53]].<ref name="pmid17970695">{{cite journal | vauthors = Obad S, Olofsson T, Mechti N, Gullberg U, Drott K | title = Regulation of the interferon-inducible p53 target gene TRIM22 (Staf50) in human T lymphocyte activation | journal = J. Interferon Cytokine Res. | volume = 27 | issue = 10 | pages = 857–64 | date = October 2007 | pmid = 17970695 | doi = 10.1089/jir.2006.0180 | url = http://luur.lub.lu.se/luur?func=downloadFile&fileOId=548138 | issn = }}{{Dead link|date=June 2018 |bot=InternetArchiveBot |fix-attempted=no }}</ref>


TRIM22 possesses [[ubiquitin ligase|E3 ubiquitin ligase]] activity and is able to [[Ubiquitin#Ubiquitination .28ubiquitylation.29|ubiquitinate]] itself with the assistance of the E2 enzyme [[UBE2D2|UbcH5B]].  Furthermore TRIM22 is located in the nucleus and therefore may function as a nuclear E3 ubiquitin ligase.<ref name="pmid18656448">{{cite journal | vauthors = Duan Z, Gao B, Xu W, Xiong S | title = Identification of TRIM22 as a RING finger E3 ubiquitin ligase | journal = Biochem. Biophys. Res. Commun. | volume = 374 | issue = 3 | pages = 502–6 |date=September 2008 | pmid = 18656448 | doi = 10.1016/j.bbrc.2008.07.070 | url = | issn = }}<!--| accessdate = 2009-02-22--></ref>
TRIM22 possesses [[ubiquitin ligase|E3 ubiquitin ligase]] activity and is able to [[Ubiquitin#Ubiquitination .28ubiquitylation.29|ubiquitinate]] itself with the assistance of the E2 enzyme [[UBE2D2|UbcH5B]].  Furthermore, TRIM22 is located in the nucleus and therefore may function as a nuclear E3 ubiquitin ligase.<ref name="pmid18656448">{{cite journal | vauthors = Duan Z, Gao B, Xu W, Xiong S | title = Identification of TRIM22 as a RING finger E3 ubiquitin ligase | journal = Biochem. Biophys. Res. Commun. | volume = 374 | issue = 3 | pages = 502–6 |date=September 2008 | pmid = 18656448 | doi = 10.1016/j.bbrc.2008.07.070 | url = | issn = }}<!--| accessdate = 2009-02-22--></ref>


== Clinical significance ==
== Clinical significance ==
Line 12: Line 12:
The protein down-regulates transcription from the [[Subtypes of HIV|HIV-1]] [[long terminal repeat]] promoter region, suggesting that function of this protein may be to mediate interferon's antiviral effects.<ref name="entrez"/><ref name="pmid7797467">{{cite journal | vauthors = Tissot C, Mechti N | title = Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression | journal = J. Biol. Chem. | volume = 270 | issue = 25 | pages = 14891–8 |date=June 1995 | pmid = 7797467 | doi = 10.1074/jbc.270.25.14891| url = http://www.jbc.org/cgi/content/full/270/25/14891 | issn = }}</ref> Other proteins that function to restrict HIV replication include [[TRIM5alpha]] and [[APOBEC3G]].<ref name="pmid18976920">{{cite journal | vauthors = Huthoff H, Towers GJ | title = Restriction of retroviral replication by APOBEC3G/F and TRIM5alpha | journal = Trends Microbiol. | volume = 16 | issue = 12 | pages = 612–9 |date=December 2008 | pmid = 18976920 | doi = 10.1016/j.tim.2008.08.013 | url = | issn = | pmc=3556578}}</ref>
The protein down-regulates transcription from the [[Subtypes of HIV|HIV-1]] [[long terminal repeat]] promoter region, suggesting that function of this protein may be to mediate interferon's antiviral effects.<ref name="entrez"/><ref name="pmid7797467">{{cite journal | vauthors = Tissot C, Mechti N | title = Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression | journal = J. Biol. Chem. | volume = 270 | issue = 25 | pages = 14891–8 |date=June 1995 | pmid = 7797467 | doi = 10.1074/jbc.270.25.14891| url = http://www.jbc.org/cgi/content/full/270/25/14891 | issn = }}</ref> Other proteins that function to restrict HIV replication include [[TRIM5alpha]] and [[APOBEC3G]].<ref name="pmid18976920">{{cite journal | vauthors = Huthoff H, Towers GJ | title = Restriction of retroviral replication by APOBEC3G/F and TRIM5alpha | journal = Trends Microbiol. | volume = 16 | issue = 12 | pages = 612–9 |date=December 2008 | pmid = 18976920 | doi = 10.1016/j.tim.2008.08.013 | url = | issn = | pmc=3556578}}</ref>


It has been demonstrated that treatment of cells with [[interferon type I]] inhibits [[HIV]] replication and TRIM22 is strongly up-regulated by interferon treatment.  Furthermore HIV particle release from cells depleted of TRIM22 with [[RNA interference]] is enhanced. TRIM22 appears to prevent the movement of the HIV [[Group-specific antigen|Gag]] protein to the plasma membrane and hence TRIM22 can block HIV replication in cell cultures by preventing the assembly of the virus.<ref name="urlResearchers discover gene that blocks HIV">{{cite web | url = http://www.physorg.com/news123505489.html | title = Researchers discover gene that blocks HIV | author = | date = 2008-02-29 | work = Medicine & Health / HIV & AIDS  | publisher = PhysOrg.com | pages = | archiveurl = | archivedate = | accessdate = 2009-02-22}}</ref><ref name="pmid18389079">{{cite journal | vauthors = Barr SD, Smiley JR, Bushman FD | editor1-last = Hope | editor1-first = Thomas J. | title = The interferon response inhibits HIV particle production by induction of TRIM22 | journal = PLoS Pathog. | volume = 4 | issue = 2 | pages = e1000007 |date=February 2008 | pmid = 18389079 | pmc = 2279259 | doi = 10.1371/journal.ppat.1000007 | url = | issn = }}</ref>
It has been demonstrated that treatment of cells with [[interferon type I]] inhibits [[HIV]] replication and TRIM22 is strongly up-regulated by interferon treatment.  Furthermore, HIV particle release from cells depleted of TRIM22 with [[RNA interference]] is enhanced. TRIM22 appears to prevent the movement of the HIV [[Group-specific antigen|Gag]] protein to the plasma membrane and hence TRIM22 can block HIV replication in cell cultures by preventing the assembly of the virus.<ref name="urlResearchers discover gene that blocks HIV">{{cite web | url = http://www.physorg.com/news123505489.html | title = Researchers discover gene that blocks HIV | author = | date = 2008-02-29 | work = Medicine & Health / HIV & AIDS  | publisher = PhysOrg.com | pages = | accessdate = 2009-02-22}}</ref><ref name="pmid18389079">{{cite journal | vauthors = Barr SD, Smiley JR, Bushman FD | editor1-last = Hope | editor1-first = Thomas J. | title = The interferon response inhibits HIV particle production by induction of TRIM22 | journal = PLoS Pathog. | volume = 4 | issue = 2 | pages = e1000007 |date=February 2008 | pmid = 18389079 | pmc = 2279259 | doi = 10.1371/journal.ppat.1000007 | url = | issn = }}</ref>


==References==
==References==

Latest revision as of 22:52, 15 June 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Tripartite motif-containing 22, also known as TRIM22, is a protein which in humans is encoded by the TRIM22 gene.[1][2][3]

Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family.[4] The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the cytoplasm and its expression is induced by interferon.[1] TRIM22 is also a target gene of the tumor suppressor protein p53.[5]

TRIM22 possesses E3 ubiquitin ligase activity and is able to ubiquitinate itself with the assistance of the E2 enzyme UbcH5B. Furthermore, TRIM22 is located in the nucleus and therefore may function as a nuclear E3 ubiquitin ligase.[6]

Clinical significance

The protein down-regulates transcription from the HIV-1 long terminal repeat promoter region, suggesting that function of this protein may be to mediate interferon's antiviral effects.[1][2] Other proteins that function to restrict HIV replication include TRIM5alpha and APOBEC3G.[7]

It has been demonstrated that treatment of cells with interferon type I inhibits HIV replication and TRIM22 is strongly up-regulated by interferon treatment. Furthermore, HIV particle release from cells depleted of TRIM22 with RNA interference is enhanced. TRIM22 appears to prevent the movement of the HIV Gag protein to the plasma membrane and hence TRIM22 can block HIV replication in cell cultures by preventing the assembly of the virus.[8][9]

References

  1. ↑ 1.0 1.1 1.2 "Entrez Gene: TRIM22 tripartite motif-containing 22".
  2. ↑ 2.0 2.1 Tissot C, Mechti N (June 1995). "Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression". J. Biol. Chem. 270 (25): 14891–8. doi:10.1074/jbc.270.25.14891. PMID 7797467.
  3. ↑ Gongora C, Tissot C, Cerdan C, Mechti N (November 2000). "The interferon-inducible Staf50 gene is downregulated during T cell costimulation by CD2 and CD28". J. Interferon Cytokine Res. 20 (11): 955–61. doi:10.1089/10799900050198390. PMID 11096452.
  4. ↑ Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
  5. ↑ Obad S, Olofsson T, Mechti N, Gullberg U, Drott K (October 2007). "Regulation of the interferon-inducible p53 target gene TRIM22 (Staf50) in human T lymphocyte activation". J. Interferon Cytokine Res. 27 (10): 857–64. doi:10.1089/jir.2006.0180. PMID 17970695.[permanent dead link]
  6. ↑ Duan Z, Gao B, Xu W, Xiong S (September 2008). "Identification of TRIM22 as a RING finger E3 ubiquitin ligase". Biochem. Biophys. Res. Commun. 374 (3): 502–6. doi:10.1016/j.bbrc.2008.07.070. PMID 18656448.
  7. ↑ Huthoff H, Towers GJ (December 2008). "Restriction of retroviral replication by APOBEC3G/F and TRIM5alpha". Trends Microbiol. 16 (12): 612–9. doi:10.1016/j.tim.2008.08.013. PMC 3556578. PMID 18976920.
  8. ↑ "Researchers discover gene that blocks HIV". Medicine & Health / HIV & AIDS. PhysOrg.com. 2008-02-29. Retrieved 2009-02-22.
  9. ↑ Barr SD, Smiley JR, Bushman FD (February 2008). Hope TJ, ed. "The interferon response inhibits HIV particle production by induction of TRIM22". PLoS Pathog. 4 (2): e1000007. doi:10.1371/journal.ppat.1000007. PMC 2279259. PMID 18389079.

External links



Retrieved from "https://www.wikidoc.org/index.php?title=TRIM22&oldid=1527865"