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Áåëîê ãðóïïû Polycomb EED (ýìáðèîíàëüíîãî ðàçâèòèÿ ýêòîäåðìû) (àíãë. Polycomb protein EED) — áåëîê, êîäèðóåìûé ó ÷åëîâåêà ãåíîì EED[1][2][3].
Ñîäåðæàíèå
Ôóíêöèè
Áåëîê Polycomb EED ÿâëÿåòñÿ ÷ëåíîì ñåìåéñòâà Polycomb (PcG). ×ëåíû ñåìåéñòâà PcG îáðàçóþò ìíîãîìåðíûå áåëêîâûå êîìïëåêñû, êîòîðûå ó÷àñòâóþò â ïîääåðæàíèè òðàíñêðèïöèîííî-ðåïðåññèâíîãî ñîñòîÿíèÿ ãåíîâ â õîäå ïîñëåäîâàòåëüíûõ êëåòî÷íûõ ïîêîëåíèé. Ýòîò áåëîê âçàèìîäåéñòâóåò ñ óñèëèòåëåì zeste 2, öèòîïëàçìàòè÷åñêèì õâîñòîì èíòåãðèíà 7, áåëêîì MÀ âèðóñà èììóíîäåôèöèòà òèïà 1 (ÂÈ×-1) è ãèñòîíäåàöåòèëàçàìè. Ýòîò áåëîê îïîñðåäóåò ïîäàâëåíèå àêòèâíîñòè ãåíîâ ãèñòîíîâ ïîñðåäñòâîì äåàöåòèëèðîâàíèÿ è ìîæåò âûñòóïàòü â êà÷åñòâå ñïåöèôè÷íîãî ðåãóëÿòîðà ôóíêöèè èíòåãðèíà. Äëÿ ýòîãî ãåíà áûëè îïðåäåëåíû äâà âàðèàíòà òðàíñêðèïòîâ, êîäèðóþùèõ ðàçëè÷íûå èçîôîðìû[3].
Êëèíè÷åñêîå çíà÷åíèå
Ó ÷åëîâåêà ìóòàöèÿ de novo[àíãë.] â EED, êàê ñîîáùàëîñü, ïðèâîäèò ê ðàçâèòèþ ñèìïòîìîâ, íàïîìèíàþùèõ ñèíäðîì Óèâåðà[4].
Âçàèìîäåéñòâèÿ ñ äðóãèìè áåëêàìè
EED, êàê áûëî âûÿâëåíî, âçàèìîäåéñòâóåò ñ:
Ïðèìå÷àíèÿ
- 1 2 Rietzler M., Bittner M., Kolanus W., Schuster A., Holzmann B. The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins. (àíãë.) // The Journal of biological chemistry. — 1998. — Vol. 273, no. 42. — P. 27459—27466. — PMID 9765275.
- Schumacher A., Lichtarge O., Schwartz S., Magnuson T. The murine Polycomb-group gene eed and its human orthologue: functional implications of evolutionary conservation. (àíãë.) // Genomics. — 1998. — Vol. 54, no. 1. — P. 79—88. — doi:10.1006/geno.1998.5509. — PMID 9806832.
- 1 2 Entrez Gene: EED embryonic ectoderm development (íåîïð.).
- Cohen A. S., Tuysuz B., Shen Y., Bhalla S. K., Jones S. J., Gibson W. T. A novel mutation in EED associated with overgrowth. (àíãë.) // Journal of human genetics. — 2015. — doi:10.1038/jhg.2015.26. — PMID 25787343.
- 1 2 3 van der Vlag J., Otte A. P. Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. (àíãë.) // Nature genetics. — 1999. — Vol. 23, no. 4. — P. 474—478. — doi:10.1038/70602. — PMID 10581039.
- van Lohuizen M., Tijms M., Voncken J. W., Schumacher A., Magnuson T., Wientjens E. Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 6. — P. 3572—3579. — PMID 9584197.
- Denisenko O., Shnyreva M., Suzuki H., Bomsztyk K. Point mutations in the WD40 domain of Eed block its interaction with Ezh2. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 10. — P. 5634—5642. — PMID 9742080.
- Jin Q., van Eynde A., Beullens M., Roy N., Thiel G., Stalmans W., Bollen M. The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor. (àíãë.) // The Journal of biological chemistry. — 2003. — Vol. 278, no. 33. — P. 30677—30685. — doi:10.1074/jbc.M302273200. — PMID 12788942.
- Ennl I., Ppai G., Cserpn I., Udvardy A., Jeang K. T., Boros I. Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus. (àíãë.) // Biochemical and biophysical research communications. — 2003. — Vol. 309, no. 1. — P. 44—51. — PMID 12943661.
Ëèòåðàòóðà- Joseph A. M., Kumar M., Mitra D. Nef: "necessary and enforcing factor" in HIV infection. (àíãë.) // Current HIV research. — 2005. — Vol. 3, no. 1. — P. 87—94. — PMID 15638726.
- Van Maele B., Debyser Z. HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. (àíãë.) // AIDS reviews. — 2005. — Vol. 7, no. 1. — P. 26—43. — PMID 15875659.
- Jones C. A., Ng J., Peterson A. J., Morgan K., Simon J., Jones R. S. The Drosophila esc and E(z) proteins are direct partners in polycomb group-mediated repression. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 5. — P. 2825—2834. — PMID 9566901.
- van Lohuizen M., Tijms M., Voncken J. W., Schumacher A., Magnuson T., Wientjens E. Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 6. — P. 3572—3579. — PMID 9584197.
- Sewalt R. G., van der Vlag J., Gunster M. J., Hamer K. M., den Blaauwen J. L., Satijn D. P., Hendrix T., van Driel R., Otte A. P. Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 6. — P. 3586—3595. — PMID 9584199.
- Denisenko O., Shnyreva M., Suzuki H., Bomsztyk K. Point mutations in the WD40 domain of Eed block its interaction with Ezh2. (àíãë.) // Molecular and cellular biology. — 1998. — Vol. 18, no. 10. — P. 5634—5642. — PMID 9742080.
- Peytavi R., Hong S. S., Gay B., d'Angeac AD, Selig L., Bnichou S., Benarous R., Boulanger P. HEED, the product of the human homolog of the murine eed gene, binds to the matrix protein of HIV-1. (àíãë.) // The Journal of biological chemistry. — 1999. — Vol. 274, no. 3. — P. 1635—1645. — PMID 9880543.
- van der Vlag J., Otte A. P. Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. (àíãë.) // Nature genetics. — 1999. — Vol. 23, no. 4. — P. 474—478. — doi:10.1038/70602. — PMID 10581039.
- Satijn D. P., Hamer K. M., den Blaauwen J., Otte A. P. The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos. (àíãë.) // Molecular and cellular biology. — 2001. — Vol. 21, no. 4. — P. 1360—1369. — doi:10.1128/MCB.21.4.1360-1369.2001. — PMID 11158321.
- Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. (àíãë.) // Genes & development. — 2002. — Vol. 16, no. 22. — P. 2893—2905. — doi:10.1101/gad.1035902. — PMID 12435631.
- Jin Q., van Eynde A., Beullens M., Roy N., Thiel G., Stalmans W., Bollen M. The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor. (àíãë.) // The Journal of biological chemistry. — 2003. — Vol. 278, no. 33. — P. 30677—30685. — doi:10.1074/jbc.M302273200. — PMID 12788942.
- Ennl I., Ppai G., Cserpn I., Udvardy A., Jeang K. T., Boros I. Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus. (àíãë.) // Biochemical and biophysical research communications. — 2003. — Vol. 309, no. 1. — P. 44—51. — PMID 12943661.
- Violot S., Hong S. S., Rakotobe D., Petit C., Gay B., Moreau K., Billaud G., Priet S., Sire J., Schwartz O., Mouscadet J. F., Boulanger P. The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1. (àíãë.) // Journal of virology. — 2003. — Vol. 77, no. 23. — P. 12507—12522. — PMID 14610174.
- Witte V., Laffert B., Rosorius O., Lischka P., Blume K., Galler G., Stilper A., Willbold D., D'Aloja P., Sixt M., Kolanus J., Ott M., Kolanus W., Schuler G., Baur A. S. HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane. (àíãë.) // Molecular cell. — 2004. — Vol. 13, no. 2. — P. 179—190. — PMID 14759364.
- Cao R., Zhang Y. SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. (àíãë.) // Molecular cell. — 2004. — Vol. 15, no. 1. — P. 57—67. — doi:10.1016/j.molcel.2004.06.020. — PMID 15225548.
- Pasini D., Bracken A. P., Jensen M. R., Lazzerini Denchi E., Helin K. Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. (àíãë.) // The EMBO journal. — 2004. — Vol. 23, no. 20. — P. 4061—4071. — doi:10.1038/sj.emboj.7600402. — PMID 15385962.
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