Pik3r1
(Перенаправлен из p85a )
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| Псевдонимы | PIK3R1 , AGM7, GRB1, IMD36, P85, P85-Alpha, Фосфоинозитид-3-киназа регуляторная субъединица 1, PI3KR1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Внешние идентификаторы | Омим : 171833 ; MGI : 97583 ; Гомологен : 7889 ; GeneCards : Pik3r1 ; OMA : pik3r1 - ортологи | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Фосфатидилинозитол 3-киназа Регуляторная субъединица Альфа -это фермент , который у людей кодируется PIK3R1 геном . [ 5 ]
Функция
[ редактировать ]Фосфатидилинозитол 3-киназа фосфорилирует иннозитол- кольцо фосфатидилинозитола в 3-х положении. Фермент содержит каталитическую субъединицу 110 кДа и регуляторную субъединицу 85, 55 или 50 кДа. Локус гена PIK3R1 кодирует регуляторную субъединицу 85 кДа, а также регуляторные субъединицы 55 и 50 кДа. Раньше считалось, что альтернативный сплайсинг этого гена привел к трем вариантам транскрипта, кодирующих различные изоформы. [ 6 ] Фактически, с тех пор было показано, что 55 и 50 кД субъединиц имеют свои собственные промотчики в генном локусе pik3r1 . [ 7 ]
Phosphatidylinositol 3-kinase plays an important role in the metabolic actions of insulin, and a mutation in this gene has been associated with insulin resistance.[8] Suppression specifically of the 85kD subunit in early murine embryoid body development results in a transient cell-cell adhesion deficiency, mediated by transient downregulation of the adhesion molecule integrin-beta1 (ITGB1).[7]
Clinical significance
[edit]Mutations in PIK3R1 are implicated in cases of breast cancer.[9]
Mutations in PIK3R1 are associated to SHORT syndrome.[10]
Interactions
[edit]PIK3R1 has been shown to interact with:
- ADAM12,[11]
- BCAR1,[12]
- CBLB,[13][14]
- CD117,[15][16][17]
- CD28,[18]
- CD7,[19][20]
- CENTG1,[21]
- CBL,[22][23][24]
- EPHA2,[25]
- EPOR,[26][27]
- ERBB3,[28][29]
- EZR,[30]
- FCGR2A,[31][32]
- GAB1,[33][34][35]
- GAB2,[36][37]
- Grb2,[38][39]
- HRAS,[40][41]
- IRS1[42][43][44][45]
- IRS2,[42][46][47][48]
- IL1R1,[49]
- JAK2,[50]
- KHDRBS1,[51][52]
- LTK,[53][54]
- LAT,[55]
- LCP2,[56]
- PIK3CD,[57]
- PTK2,[58]
- SHB,[59]
- TUBA1B,[60]
- TYRO3,[61]
- VAV1,[26][33] and
- WAS.[62]
References
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Further reading
[edit]- Benito M, Valverde AM, Lorenzo M (1996). "IGF-I: a mitogen also involved in differentiation processes in mammalian cells". Int. J. Biochem. Cell Biol. 28 (5): 499–510. doi:10.1016/1357-2725(95)00168-9. PMID 8697095.
- Snapper SB, Rosen FS (1999). "The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization". Annu. Rev. Immunol. 17: 905–29. doi:10.1146/annurev.immunol.17.1.905. PMID 10358777.
- Катада Т., Куросу Х., Окада Т., Сузуки Т., Цудзимото Н., Такасуга С., Контани К, Хазеки О., UI M (1999). «Синергетическая активация семейства фосфоинозитид-3-киназы посредством G-белкового соединения и рецепторов, связанных с тирозинкиназой». Химический Физический Липиды . 98 (1–2): 79–86. doi : 10.1016/s0009-3084 (99) 00020-1 . PMID 10358930 .
- Zhang W, Samelson LE (2000). «Роль адаптеров, связанных с мембраной в передаче сигналов рецептора Т-клеток» . Семин Иммунол . 12 (1): 35–41. doi : 10.1006/smim.2000.0205 . PMID 10723796 .
- Гринвей А.Л., Холлоуэй Г., Макфи Д.А., Эллис П., Корналл А., Лидман М. (2003). «Контроль NEF NEF ВИЧ-1 молекул передачи сигналов клеток: множественные стратегии для стимулирования репликации вируса». J. Biosci . 28 (3): 323–35. doi : 10.1007/bf02970151 . PMID 12734410 . S2CID 33749514 .
- Leavitt SA, Schon A, Klein JC, Manjappara U, Chaiken IM, Freire E (2004). «Взаимодействие белков ВИЧ-1 GP120 и NEF с клеточными партнерами определяют новую аллостерическую парадигму». Карт Белковый пепт. Наука 5 (1): 1–8. doi : 10.2174/138920303043486955 . PMID 14965316 .
- Джозеф А.М., Кумар М., Митра Д. (2005). «NEF:« Необходимый и принудительный фактор »при ВИЧ -инфекции». Карт ВИЧ РЕС . 3 (1): 87–94. doi : 10.2174/1570162052773013 . PMID 15638726 .
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