TRIM25: Difference between revisions

'''Tripartite motif-containing protein 25''' is a [[protein]] that in humans is encoded by the ''TRIM25'' [[gene]].<ref name="pmid7789997">{{cite journal | vauthors = Inoue S, Orimo A, Matsuda Y, Inazawa J, Emi M, Nakamura Y, Hori T, Muramatsu M | title = Chromosome mapping of human (ZNF147) and mouse genes for estrogen-responsive finger protein (efp), a member of the RING finger family | journal = Genomics | volume = 25 | issue = 2 | pages = 581–3 | date = Jan 1995 | pmid = 7789997 | pmc = | doi = 10.1016/0888-7543(95)80064-S }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIM25 tripartite motif-containing 25| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7706| accessdate = }}</ref>

TRIM25 has an N-terminal RING domain, followed by a B-box type 1 domain, a B-box type 2 domain, a coiled-coil domain (CCD) and a C-terminal SPRY domain. The RING domain coordinates two zinc atoms and is essential for recruiting [[ubiquitin-conjugating enzyme]]s. The function of the B-box domains is unknown. The CCD domain has been implicated in multimerization and other protein-protein interactions.<ref>{{cite journal | vauthors = Haik KG | title = Visual difficulties from video display terminals | journal = Southern Medical Journal | volume = 78 | issue = 7 | pages = 887–8 | date = Jul 1985 | pmc = | doi=10.1097/00007611-198507000-00031 | pmid=4012390}}</ref> The SPRY domain is required for substrate recruitment.<ref>{{cite journal | vauthors = Pilka L, Trávník P, Dvorák M, Tesarík J, Ventruba P, Krejcí K, Soska J | title = [Delivery after intrauterine embryo transfer obtained by fertilization and oocyte culture in vitro] | journal = Ceskoslovenská Gynekologie | volume = 50 | issue = 7 | pages = 452–9 | date = Aug 1985 | pmid = 4042170 }}</ref> The NMR chemical shifts for backbone of the PRYSPRY domain of TRIM25 is assigned based on triple-resonance experiments using uniformly isotopic labeled protein and the secondary structure of the domain PRYSPRY domain of TRIM25 predicted based on the NMR assignments.<ref>{{Cite journal|lastlast1 = Kong|firstfirst1 = Chen|last2 = Penumutchu|first2 = Srinivasa R.|last3 = Hung|first3 = Kuo-wei|last4 = Huang|first4 = Huiying|last5 = Lin|first5 = Tianwei|last6 = Yu|first6 = Chin|date = 2015-02-22|title = Backbone resonance assignments of the PRYSPRY domain of TRIM25|url = https://link.springer.com/article/10.1007/s12104-015-9599-x|journal = Biomolecular NMR Assignments|language = en|volume = 9|issue = 2|pages = 313–315|doi = 10.1007/s12104-015-9599-x|pmid = 25702035|s2cid = 11475584|issn = 1874-2718}}</ref>

TRIM25 plays a key role in the [[RIG-I]] signaling pathway. RIG-I is a cytosolic [[pattern recognition receptor]] that senses viral RNA. Following RNA recognition, the [[caspase recruitment domain]] (CARD) of RIG-I undergoes K(63)-linked [[ubiquitination]] by TRIM25. The RING and SPRY domains of TRIM25 mediate its interaction with RIG-I. IFN production then follows by an intracellular signaling pathway involving [[IRF3]].<ref>{{cite journal | vauthors = Gack MU, Kirchhofer A, Shin YC, Inn KS, Liang C, Cui S, Myong S, Ha T, Hopfner KP, Jung JU | title = Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 43 | pages = 16743–8 | date = Oct 2008 | pmid = 18948594 | doi = 10.1073/pnas.0804947105 | pmc=2575490| doi-access = free }}</ref>

To avoid IFN production, the non structural protein ([[NS1 influenza protein|NS1]]) of [[influenza]] will interact with CCD domain of TRIM25 to block RIG-I ubiquitination. Some studies have shown that a deletion of the CCD domain of TRIM25 prevents the binding of NS1.<ref>{{cite journal | vauthors = Gack MU, Albrecht RA, Urano T, Inn KS, Huang IC, Carnero E, Farzan M, Inoue S, Jung JU, García-Sastre A | title = Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I | journal = Cell Host & Microbe | volume = 5 | issue = 5 | pages = 439–49 | date = May 2009 | pmid = 19454348 | doi = 10.1016/j.chom.2009.04.006 | pmc=2737813}}</ref> Without this ubiquitination, there won’t be IFN production.

* {{cite journal | vauthors = Horie K, Urano T, Ikeda K, Inoue S | title = Estrogen-responsive RING finger protein controls breast cancer growth | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 85 | issue = 2-52–5 | pages = 101–4 | date = Jun 2003 | pmid = 12943693 | doi = 10.1016/S0960-0760(03)00209-7 | s2cid = 22487508 }}

* {{cite journal | vauthors = Inoue S, Orimo A, Hosoi T, Kondo S, Toyoshima H, Kondo T, Ikegami A, Ouchi Y, Orimo H, Muramatsu M | title = Genomic binding-site cloning reveals an estrogen-responsive gene that encodes a RING finger protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 90 | issue = 23 | pages = 11117–21 | date = Dec 1993 | pmid = 8248217 | pmc = 47933 | doi = 10.1073/pnas.90.23.11117 | doi-access = free }}

* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 | doi-access = free }}

* {{cite journal | vauthors = Ikeda K, Orimo A, Higashi Y, Muramatsu M, Inoue S | title = Efp as a primary estrogen-responsive gene in human breast cancer | journal = FEBS Letters | volume = 472 | issue = 1 | pages = 9–13 | date = Apr 2000 | pmid = 10781795 | doi = 10.1016/S0014-5793(00)01421-6 | s2cid = 10570937 | doi-access = free }}

* {{cite journal | vauthors = Urano T, Saito T, Tsukui T, Fujita M, Hosoi T, Muramatsu M, Ouchi Y, Inoue S | title = Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth | journal = Nature | volume = 417 | issue = 6891 | pages = 871–5 | date = Jun 2002 | pmid = 12075357 | doi = 10.1038/nature00826 | bibcode = 2002Natur.417..871U | s2cid = 4348545 }}

* {{cite journal | vauthors = Shimada N, Suzuki T, Inoue S, Kato K, Imatani A, Sekine H, Ohara S, Shimosegawa T, Sasano H | title = Systemic distribution of estrogen-responsive finger protein (Efp) in human tissues | journal = Molecular and Cellular Endocrinology | volume = 218 | issue = 1-21–2 | pages = 147–53 | date = Apr 2004 | pmid = 15130519 | doi = 10.1016/j.mce.2003.12.008 | s2cid = 44761828 }}

* {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = Jan 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 | s2cid = 7200157 }}

* {{cite journal | vauthors = Suzuki T, Urano T, Tsukui T, Horie-Inoue K, Moriya T, Ishida T, Muramatsu M, Ouchi Y, Sasano H, Inoue S | title = Estrogen-responsive finger protein as a new potential biomarker for breast cancer | journal = Clinical Cancer Research | volume = 11 | issue = 17 | pages = 6148–54 | date = Sep 2005 | pmid = 16144914 | doi = 10.1158/1078-0432.CCR-05-0040 | doi-access = | s2cid = 11698115 }}

* {{cite journal | vauthors = Nakayama H, Sano T, Motegi A, Oyama T, Nakajima T | title = Increasing 14-3-3 sigma expression with declining estrogen receptor alpha and estrogen-responsive finger protein expression defines malignant progression of endometrial carcinoma | journal = Pathology International | volume = 55 | issue = 11 | pages = 707–15 | date = Nov 2005 | pmid = 16271083 | doi = 10.1111/j.1440-1827.2005.01900.x | s2cid = 7106422 }}

* {{cite journal | vauthors = Nakajima A, Maruyama S, Bohgaki M, Miyajima N, Tsukiyama T, Sakuragi N, Hatakeyama S | title = Ligand-dependent transcription of estrogen receptor alpha is mediated by the ubiquitin ligase EFP | journal = Biochemical and Biophysical Research Communications | volume = 357 | issue = 1 | pages = 245–51 | date = May 2007 | pmid = 17418098 | doi = 10.1016/j.bbrc.2007.03.134 | hdl = 2115/24261 | hdl-access = free }}