PKD2

Wikipedia — ирекле энциклопедия проектыннан ([http://tt.wikipedia.org.ttcysuttlart1999.aylandirow.tmf.org.ru/wiki/PKD2 latin yazuında])
PKD2
Нинди таксонда бар H. sapiens[d][1]
Кодлаучы ген PKD2[d][1]
Молекуляр функция transmembrane transporter binding[d][2], cytoskeletal protein binding[d][3], signaling receptor binding[d][4][5], muscle alpha-actinin binding[d][5], связывание с ионом металла[d][5], HLH domain binding[d][6], voltage-gated cation channel activity[d][7], гомодимеризация белка[d][8], calcium-induced calcium release activity[d][9], channel activity[d][5], связывание с белками плазмы[d][10][11][12][…], actinin binding[d][13], voltage-gated calcium channel activity[d][14][7], calcium channel activity[d][5][5], phosphoprotein binding[d][15], alpha-actinin binding[d][5], связывание похожих белков[d][5][16][17][…], ATPase binding[d][5][5], calcium ion binding[d][5][5][5][…], outward rectifier potassium channel activity[d][5][5], voltage-gated sodium channel activity[d][18][7], voltage-gated potassium channel activity[d][18], potassium channel activity[d][5][5][5][…] һәм voltage-gated ion channel activity[d][5][9]
Күзәнәк компоненты filamentous actin[d][19], мембрана[d][5][5][5], integral component of cytoplasmic side of endoplasmic reticulum membrane[d][20], cell projection[d][5], экзосома[d][21], lamellipodium[d][3], мембрана өлеше[d][5], basal plasma membrane[d][22], integral component of lumenal side of endoplasmic reticulum membrane[d][20], ciliary membrane[d][5][5], polycystin complex[d][5][5], реснички[d][5][5][5], күзәнәк мембранасы[d][5][5][14][…], cell-cell junction[d][5][5], ciliary basal body[d][5][23], эндоплазматик челтәр[4][5][5][…], basal cortex[d][5][22], mitotic spindle[d][5][24], цитоплазма[6][5][22], motile cilium[d][5][5], non-motile cilium[d][5][5], күзәнәк мембранасы өлеше[d][18][25][26][…], endoplasmic reticulum membrane[d][5][27][9], basolateral plasma membrane[d][5], cytoplasmic vesicle membrane[d][5] һәм цитоплазматическая везикула[d][5]
Биологик процесс regulation of calcium ion import[d][9], cellular response to osmotic stress[d][19], negative regulation of G1/S transition of mitotic cell cycle[d][6], heart looping[d][28], metanephric S-shaped body morphogenesis[d][29], негативная регуляция пролиферации клеток[d][30], mesonephric tubule development[d][29], развитие почечной системы[d][5], metanephric cortex development[d][29], нефрогенез[d][5], cytoplasmic sequestering of transcription factor[d][6], ion transport[d][5], metanephric ascending thin limb development[d][29], branching involved in ureteric bud morphogenesis[d][29], развитие нервной трубки[d][29], арка мие үсеше[d][29], metanephric distal tubule development[d][29], centrosome duplication[d][31], cellular calcium ion homeostasis[d][5], determination of liver left/right asymmetry[d][28], cellular response to fluid shear stress[d][32][5], aorta development[d][29], cellular response to hydrostatic pressure[d][19], metanephric mesenchyme development[d][29], renal artery morphogenesis[d][29], metanephric cortical collecting duct development[d][29], mesonephric duct development[d][29], positive regulation of cytosolic calcium ion concentration[d][5], positive regulation of nitric oxide biosynthetic process[d][32][5], cellular response to reactive oxygen species[d][33], positive regulation of gene expression[d][5], metanephric part of ureteric bud development[d][29], regulation of cell population proliferation[d][27], metanephric smooth muscle tissue development[d][29], positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity[d][4], положительная регуляция транскрипции РНК полимеразой II промотор[d][8][6], йөрәк үсеше[d][29][5], receptor signaling pathway via JAK-STAT[d][5][5], detection of mechanical stimulus[d][5][5][5], embryonic placenta development[d][5][5], detection of nodal flow[d][5][5], развитие печени[d][29][5], placenta blood vessel development[d][5][5], renal tubule morphogenesis[d][5][5], determination of left/right symmetry[d][5][5], постсинаптический потенциал[d][5], negative regulation of ryanodine-sensitive calcium-release channel activity[d][5][5], calcium ion transport[d][5][5][5][…], release of sequestered calcium ion into cytosol[d][32][5][9], calcium ion transmembrane transport[d][5][5][9], cellular response to calcium ion[d][5][5], sodium ion transmembrane transport[d][18][7], protein homotetramerization[d][26], cellular response to cAMP[d][25], potassium ion transmembrane transport[d][5][18][5][…], potassium ion transport[d][5], regulation of ion transmembrane transport[d][5] һәм перенос[d][5]

PKD2 (ингл. ) — аксымы, шул ук исемдәге ген тарафыннан кодлана торган югары молекуляр органик матдә.[34][35]

Искәрмәләр[үзгәртү | вики-текстны үзгәртү]

  1. ↑ 1,0 1,1 UniProt
  2. ↑ L Tsiokas, T Arnould, C Zhu et al. Specific association of the gene product of PKD2 with the TRPC1 channel // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1999. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.96.7.3934 — PMID:10097141
  3. ↑ 3,0 3,1 Gallagher A. R., A Cedzich, N Gretz et al. The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2000. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.97.8.4017 — PMID:10760273
  4. ↑ 4,0 4,1 4,2 Guggino W. B. Polycystin 2 interacts with type I inositol 1,4,5-trisphosphate receptor to modulate intracellular Ca2+ signaling // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2005. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M510082200 — PMID:16223735
  5. ↑ 5,00 5,01 5,02 5,03 5,04 5,05 5,06 5,07 5,08 5,09 5,10 5,11 5,12 5,13 5,14 5,15 5,16 5,17 5,18 5,19 5,20 5,21 5,22 5,23 5,24 5,25 5,26 5,27 5,28 5,29 5,30 5,31 5,32 5,33 5,34 5,35 5,36 5,37 5,38 5,39 5,40 5,41 5,42 5,43 5,44 5,45 5,46 5,47 5,48 5,49 5,50 5,51 5,52 5,53 5,54 5,55 5,56 5,57 5,58 5,59 5,60 5,61 5,62 5,63 5,64 5,65 5,66 5,67 5,68 5,69 5,70 5,71 5,72 5,73 5,74 5,75 5,76 5,77 5,78 5,79 5,80 5,81 5,82 5,83 5,84 5,85 5,86 5,87 5,88 5,89 GOA
  6. ↑ 6,0 6,1 6,2 6,3 6,4 Li X., Luo Y., Starremans P. G. et al. Polycystin-1 and polycystin-2 regulate the cell cycle through the helix-loop-helix inhibitor Id2 // Nat. Cell Biol. — NPG, 2005. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB1326 — PMID:16311606
  7. ↑ 7,0 7,1 7,2 7,3 S González-Perrett, K Kim, C Ibarra et al. Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2001. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.98.3.1182 — PMID:11252306
  8. ↑ 8,0 8,1 L Tsiokas, E Kim, T Arnould et al. Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2 // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 1997. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.94.13.6965 — PMID:9192675
  9. ↑ 9,0 9,1 9,2 9,3 9,4 9,5 Koulen P. Polycystin-2 is an intracellular calcium release channel // Nat. Cell Biol. — NPG, 2002. — ISSN 1465-7392; 1476-4679 — doi:10.1038/NCB754 — PMID:11854751
  10. ↑ Li Q., Shen P. Y., Wu G. et al. Polycystin-2 interacts with troponin I, an angiogenesis inhibitor // Biochemistry / A. Schepartz — ACS, 2003. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI0267792 — PMID:12525172
  11. ↑ Li Q., Liu Y., Shen P. Y. et al. Troponin I binds polycystin-L and inhibits its calcium-induced channel activation // Biochemistry / A. Schepartz — ACS, 2003. — ISSN 0006-2960; 1520-4995; 1943-295X — doi:10.1021/BI034210A — PMID:12809519
  12. ↑ Witzgall R. PIGEA-14, a novel coiled-coil protein affecting the intracellular distribution of polycystin-2 // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M314206200 — PMID:15194699
  13. ↑ Montalbetti N. Alpha-actinin associates with polycystin-2 and regulates its channel activity // Human Molecular Genetics — OUP, 2005. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDI167 — PMID:15843396
  14. ↑ 14,0 14,1 Schermer B., Benzing T., Kramer-Zucker A. Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation // EMBO J. — NPG, 2005. — ISSN 0261-4189; 1460-2075 — doi:10.1038/SJ.EMBOJ.7600566 — PMID:15692563
  15. ↑ Kramer-Zucker A. PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation // Human Molecular Genetics — OUP, 2010. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDP463 — PMID:19801576
  16. ↑ Leandro C de Oliveira, Germino G. Macromolecular assembly of polycystin-2 intracytosolic C-terminal domain // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2011. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1106766108 — PMID:21622852
  17. ↑ Yu Y., Tong L. Structural and molecular basis of the assembly of the TRPP2/PKD1 complex // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2009. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.0903684106 — PMID:19556541
  18. ↑ 18,0 18,1 18,2 18,3 18,4 Møller S. G., Yu Y. Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant // Proc. Natl. Acad. Sci. U.S.A. / M. R. Berenbaum — [Washington, etc.], USA: National Academy of Sciences [etc.], 2016. — ISSN 0027-8424; 1091-6490 — doi:10.1073/PNAS.1517066113 — PMID:27071085
  19. ↑ 19,0 19,1 19,2 Montalbetti N. Effect of hydro-osmotic pressure on polycystin-2 channel function in the human syncytiotrophoblast // Pflügers Archiv: European Journal of Physiology — Springer Science+Business Media, 2005. — ISSN 0031-6768; 1432-2013; 0365-267X — doi:10.1007/S00424-005-1458-7 — PMID:16025301
  20. ↑ 20,0 20,1 Hoffmeister H., Gallagher A., Rascle A. et al. The human polycystin-2 protein represents an integral membrane protein with six membrane-spanning domains and intracellular N- and C-termini // Biochem. J. — London [etc.]: Portland Press, 2011. — ISSN 0264-6021; 1470-8728 — doi:10.1042/BJ20101141 — PMID:21044049
  21. ↑ Pisitkun T., Tchapyjnikov D., Knepper M. A. Large-scale proteomics and phosphoproteomics of urinary exosomes // Journal of the American Society of Nephrology / J. Briggs — American Society of Nephrology, 2008. — ISSN 1046-6673; 1533-3450 — doi:10.1681/ASN.2008040406 — PMID:19056867
  22. ↑ 22,0 22,1 22,2 L Foggensteiner, Bevan A. P., R Thomas et al. Cellular and subcellular distribution of polycystin-2, the protein product of the PKD2 gene // Journal of the American Society of Nephrology / J. Briggs — American Society of Nephrology, 2000. — ISSN 1046-6673; 1533-3450 — PMID:10770959
  23. ↑ Jurczyk A., Gromley A., Redick S. et al. Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly // J. Cell Biol. / J. Nunnari — Rockefeller University Press, 2004. — ISSN 0021-9525; 1540-8140 — doi:10.1083/JCB.200405023 — PMID:15337773
  24. ↑ Gorbsky G. J. PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2004. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M400544200 — PMID:15123714
  25. ↑ 25,0 25,1 María del Rocío Cantero The cAMP Signaling Pathway and Direct Protein Kinase A Phosphorylation Regulate Polycystin-2 (TRPP2) Channel Function // J. Biol. Chem. / L. M. Gierasch — Baltimore [etc.]: American Society for Biochemistry and Molecular Biology, 2015. — ISSN 0021-9258; 1083-351X; 1067-8816 — doi:10.1074/JBC.M115.661082 — PMID:26269590
  26. ↑ 26,0 26,1 Kühlbrandt W., M. Gregor Madej, Pike A. et al. Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2 // Nat. Struct. Mol. Biol. — USA: NPG, 2017. — ISSN 1545-9993; 1545-9985 — doi:10.1038/NSMB.3357 — PMID:28092368
  27. ↑ 27,0 27,1 Piva R., Lambertini E. Deficiency of polycystin-2 reduces Ca2+ channel activity and cell proliferation in ADPKD lymphoblastoid cells // FASEB J. — FASEB, 2004. — ISSN 0892-6638; 1530-6860 — doi:10.1096/FJ.03-0687FJE — PMID:15001556
  28. ↑ 28,0 28,1 Bataille S., Dahan K., Burtey S. Association of PKD2 (polycystin 2) mutations with left-right laterality defects // Am. J. Kidney Dis. — Elsevier BV, 2011. — ISSN 0272-6386; 1523-6838 — doi:10.1053/J.AJKD.2011.05.015 — PMID:21719175
  29. ↑ 29,00 29,01 29,02 29,03 29,04 29,05 29,06 29,07 29,08 29,09 29,10 29,11 29,12 29,13 29,14 29,15 29,16 Attié-Bitach T., Devuyst O., Gubler M. Expression of PKD1 and PKD2 transcripts and proteins in human embryo and during normal kidney development // Am. J. Pathol. — Elsevier BV, 2002. — ISSN 0002-9440; 1525-2191; 0097-3599 — doi:10.1016/S0002-9440(10)64919-X — PMID:11891195
  30. ↑ Liang G., Yang J., Wang Z. et al. Polycystin-2 down-regulates cell proliferation via promoting PERK-dependent phosphorylation of eIF2alpha // Human Molecular Genetics — OUP, 2008. — ISSN 0964-6906; 1460-2083 — doi:10.1093/HMG/DDN221 — PMID:18664456
  31. ↑ Burtey S., Riera M., Mattéi M. Centrosome overduplication and mitotic instability in PKD2 transgenic lines // Cell Biol. Int. — Portland Press, 2008. — ISSN 1065-6995; 1095-8355 — doi:10.1016/J.CELLBI.2008.07.021 — PMID:18725310
  32. ↑ 32,0 32,1 32,2 AbouAlaiwi W. A., Takahashi M., Mell B. R. et al. Ciliary polycystin-2 is a mechanosensitive calcium channel involved in nitric oxide signaling cascades // Circ. Res. — Lippincott Williams & Wilkins, 2009. — ISSN 0009-7330; 1524-4571 — doi:10.1161/CIRCRESAHA.108.192765 — PMID:19265036
  33. ↑ N Montalbetti, Cantero M. R., Dalghi M. G. et al. Reactive oxygen species inhibit polycystin-2 (TRPP2) cation channel activity in term human syncytiotrophoblast // Placenta — Elsevier BV, 2008. — ISSN 0143-4004; 1532-3102 — doi:10.1016/J.PLACENTA.2008.02.015 — PMID:18417208
  34. ↑ HUGO Gene Nomenclature Commitee, HGNC:29223 (ингл.). әлеге чыганактан 2015-10-25 архивланды. 18 сентябрь, 2017 тикшерелгән.
  35. ↑ UniProt, Q9ULJ7 (ингл.). 18 сентябрь, 2017 тикшерелгән.

Чыганаклар[үзгәртү | вики-текстны үзгәртү]

  • Степанов В.М. (2005). Молекулярная биология. Структура и функция белков. Москва: Наука. ISBN 5-211-04971-3.(рус.)
  • Bruce Alberts, Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter (2002). Molecular Biology of the Cell (вид. 4th). Garland. ISBN 0815332181.(ингл.)


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