Notch 1

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Notch 1
Protein NOTCH1 PDB 1pb5.png
PDB rendering based on 1pb5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols NOTCH1 ; TAN1; hN1
External IDs OMIM190198 MGI97363 HomoloGene32049 GeneCards: NOTCH1 Gene
RNA expression pattern
PBB GE NOTCH1 218902 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4851 18128
Ensembl ENSG00000148400 ENSMUSG00000026923
UniProt P46531 Q01705
RefSeq (mRNA) NM_017617 NM_008714
RefSeq (protein) NP_060087 NP_032740
Location (UCSC) Chr 9:
139.39 – 139.44 Mb
Chr 2:
26.46 – 26.52 Mb
PubMed search [1] [2]

Notch homolog 1, translocation-associated (Drosophila), also known as NOTCH1, is a human gene encoding a single-pass transmembrane receptor.

Function[edit]

This gene encodes a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. Notch family members play a role in a variety of developmental processes by controlling cell fate decisions. The Notch signaling network is an evolutionarily conserved intercellular signaling pathway that regulates interactions between physically adjacent cells. In Drosophila, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signaling pathway that plays a key role in development. Homologues of the notch-ligands have also been identified in human, but precise interactions between these ligands and the human notch homologues remain to be determined. This protein is cleaved in the trans-Golgi network, and presented on the cell surface as a heterodimer. This protein functions as a receptor for membrane bound ligands, and may play multiple roles during development.[1]

A deficiency can be associated with bicuspid aortic valve.[2]

There is evidence that activated Notch 1 and Notch 3 promote differentiation of progenitor cells into astroglia.[3] Notch 1, then activated before birth, induces radial glia differentiation,[4] but postnatally induces the differentiation into astrocytes.[5] One study shows that Notch-1 cascade is activated by Reelin in an unidentified way.[6] Reelin and Notch1 cooperate in the development of the dentate gyrus, according to another.[7]

Interactions[edit]

NOTCH1 has been shown to interact with:


References[edit]

  1. ^ "Entrez Gene: NOTCH1 Notch homolog 1, translocation-associated (Drosophila)". 
  2. ^ McKellar SH, Tester DJ, Yagubyan M, Majumdar R, Ackerman MJ, Sundt TM (August 2007). "Novel NOTCH1 mutations in patients with bicuspid aortic valve disease and thoracic aortic aneurysms". J Thorac Cardiovasc Surg 134 (2): 290–296. doi:10.1016/j.jtcvs.2007.02.041. PMID 17662764. 
  3. ^ Tanigaki K, Nogaki F, Takahashi J, Tashiro K, Kurooka H, Honjo T (January 2001). "Notch1 and Notch3 instructively restrict bFGF-responsive multipotent neural progenitor cells to an astroglial fate". Neuron 29 (1): 45–55. doi:10.1016/S0896-6273(01)00179-9. PMID 11182080. 
  4. ^ Gaiano N, Nye JS, Fishell G (May 2000). "Radial glial identity is promoted by Notch1 signaling in the murine forebrain". Neuron 26 (2): 395–404. doi:10.1016/S0896-6273(00)81172-1. PMID 10839358. 
  5. ^ Chambers CB, Peng Y, Nguyen H, Gaiano N, Fishell G, Nye JS (March 2001). "Spatiotemporal selectivity of response to Notch1 signals in mammalian forebrain precursors". Development 128 (5): 689–702. PMID 11171394. 
  6. ^ Keilani S, Sugaya K (July 2008). "Reelin induces a radial glial phenotype in human neural progenitor cells by activation of Notch-1". BMC Dev. Biol. 8 (1): 69. doi:10.1186/1471-213X-8-69. PMC 2447831. PMID 18593473. 
  7. ^ Sibbe M, Förster E, Basak O, Taylor V, Frotscher M (July 2009). "Reelin and Notch1 cooperate in the development of the dentate gyrus". J. Neurosci. 29 (26): 8578–85. doi:10.1523/JNEUROSCI.0958-09.2009. PMID 19571148. 
  8. ^ Foltz DR, Santiago MC, Berechid BE, Nye JS (June 2002). "Glycogen synthase kinase-3beta modulates notch signaling and stability". Curr. Biol. 12 (12): 1006–11. doi:10.1016/s0960-9822(02)00888-6. PMID 12123574. 
  9. ^ Sade H, Krishna S, Sarin A (January 2004). "The anti-apoptotic effect of Notch-1 requires p56lck-dependent, Akt/PKB-mediated signaling in T cells". J. Biol. Chem. 279 (4): 2937–44. doi:10.1074/jbc.M309924200. PMID 14583609. 
  10. ^ Wu L, Aster JC, Blacklow SC, Lake R, Artavanis-Tsakonas S, Griffin JD (December 2000). "MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors". Nat. Genet. 26 (4): 484–9. doi:10.1038/82644. PMID 11101851. 
  11. ^ Wu L, Sun T, Kobayashi K, Gao P, Griffin JD (November 2002). "Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors". Mol. Cell. Biol. 22 (21): 7688–700. doi:10.1128/mcb.22.21.7688-7700.2002. PMC 135662. PMID 12370315. 
  12. ^ Blokzijl A, Dahlqvist C, Reissmann E, Falk A, Moliner A, Lendahl U et al. (November 2003). "Cross-talk between the Notch and TGF-beta signaling pathways mediated by interaction of the Notch intracellular domain with Smad3". J. Cell Biol. 163 (4): 723–8. doi:10.1083/jcb.200305112. PMC 2173673. PMID 14638857. 
  13. ^ Guan E, Wang J, Laborda J, Norcross M, Baeuerle PA, Hoffman T (May 1996). "T cell leukemia-associated human Notch/translocation-associated Notch homologue has I kappa B-like activity and physically interacts with nuclear factor-kappa B proteins in T cells". J. Exp. Med. 183 (5): 2025–32. doi:10.1084/jem.183.5.2025. PMC 2192574. PMID 8642313. 
  14. ^ Wang J, Shelly L, Miele L, Boykins R, Norcross MA, Guan E (July 2001). "Human Notch-1 inhibits NF-kappa B activity in the nucleus through a direct interaction involving a novel domain". J. Immunol. 167 (1): 289–95. doi:10.4049/jimmunol.167.1.289. PMID 11418662. 
  15. ^ Sakamoto K, Yamaguchi S, Ando R, Miyawaki A, Kabasawa Y, Takagi M et al. (August 2002). "The nephroblastoma overexpressed gene (NOV/ccn3) protein associates with Notch1 extracellular domain and inhibits myoblast differentiation via Notch signaling pathway". J. Biol. Chem. 277 (33): 29399–405. doi:10.1074/jbc.M203727200. PMID 12050162. 
  16. ^ Nam Y, Weng AP, Aster JC, Blacklow SC (June 2003). "Structural requirements for assembly of the CSL.intracellular Notch1.Mastermind-like 1 transcriptional activation complex". J. Biol. Chem. 278 (23): 21232–9. doi:10.1074/jbc.M301567200. PMID 12644465. 
  17. ^ Aster JC, Robertson ES, Hasserjian RP, Turner JR, Kieff E, Sklar J (April 1997). "Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jkappa or nuclear localization sequences retain the ability to associate with RBP-Jkappa and activate transcription". J. Biol. Chem. 272 (17): 11336–43. doi:10.1074/jbc.272.17.11336. PMID 9111040. 
  18. ^ Beatus P, Lundkvist J, Oberg C, Pedersen K, Lendahl U (June 2001). "The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity". Mech. Dev. 104 (1-2): 3–20. doi:10.1016/s0925-4773(01)00373-2. PMID 11404076. 
  19. ^ Zhou S, Fujimuro M, Hsieh JJ, Chen L, Miyamoto A, Weinmaster G et al. (April 2000). "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Mol. Cell. Biol. 20 (7): 2400–10. doi:10.1128/mcb.20.7.2400-2410.2000. PMC 85419. PMID 10713164. 
  20. ^ Chastagner P, Israël A, Brou C. "AIP4/Itch regulates Notch receptor degradation in the absence of ligand". PLoS ONE 3 (7): e2735. doi:10.1371/journal.pone.0002735. PMC 2444042. PMID 18628966. 
  21. ^ Yeh TS, Lin YM, Hsieh RH, Tseng MJ (October 2003). "Association of transcription factor YY1 with the high molecular weight Notch complex suppresses the transactivation activity of Notch". J. Biol. Chem. 278 (43): 41963–9. doi:10.1074/jbc.M304353200. PMID 12913000. 

Further reading[edit]

External links[edit]