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AXL receptor tyrosine kinase

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Title: AXL receptor tyrosine kinase  
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AXL receptor tyrosine kinase

AXL receptor tyrosine kinase

PDB rendering based on 2c5d.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; JTK11; UFO
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Tyrosine-protein kinase receptor UFO is an enzyme that in humans is encoded by the AXL gene. [1][2]

Contents

  • Function 1
  • Interactions 2
  • References 3
  • Further reading 4

Function

The protein encoded by this gene is a member of the receptor tyrosine kinase subfamily. Although it is similar to other receptor tyrosine kinases, the Axl protein represents a unique structure of the extracellular region that juxtaposes IgL and FNIII repeats. It transduces signals from the extracellular matrix into the cytoplasm by binding growth factors like vitamin K-dependent protein growth-arrest-specific gene 6. It is involved in the stimulation of cell proliferation. This receptor can also mediate cell aggregation by homophilic binding. Axl is a chronic myelogenous leukemia-associated oncogene and also associated with colon cancer and melanoma. It is in close vicinity to the bcl3 oncogene, which is at 19q13.1-q13.2. The Axl gene is evolutionarily conserved between vertebrate species. This gene has two different alternatively spliced transcript variants.[2]

Interactions

AXL receptor tyrosine kinase has been shown to interact with TENC1.[3] Axl is an essential epithelial-to-mesenchymal transition-induced regulator of breast cancer metastasis and patient survival.[4]

References

  1. ^ O'Bryan JP, Frye RA, Cogswell PC, Neubauer A, Kitch B, Prokop C, Espinosa R 3rd, Le Beau MM, Earp HS, Liu ET (Oct 1991). "axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase". Mol Cell Biol 11 (10): 5016–31.  
  2. ^ a b "Entrez Gene: AXL AXL receptor tyrosine kinase". 
  3. ^ Hafizi S, Alindri F, Karlsson R, Dahlbäck B (2002). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochem. Biophys. Res. Commun. 299 (5): 793–800.  
  4. ^ Vajkoczy P, Knyazev P, Kunkel A, Capelle HH, Behrndt S, von Tengg-Kobligk H, Kiessling F, Eichelsbacher U, Essig M, Read TA, Erber R, Ullrich A (2006). "Dominant-negative inhibition of the Axl receptor tyrosine kinase suppresses brain tumor cell growth and invasion and prolongs survival". Proc. Natl. Acad. Sci. U.S.A. 103 (15): 5799–804.  

Further reading

  • Neubauer A, Burchert A, Maiwald C, et al. (1997). "Recent progress on the role of Axl, a receptor tyrosine kinase, in malignant transformation of myeloid leukemias.". Leuk. Lymphoma 25 (1–2): 91–6.  
  • Bergsagel PL, Victor-Kobrin C, Timblin CR, et al. (1992). "A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed on plasma cells". J. Immunol. 148 (2): 590–6.  
  • Janssen JW, Schulz AS, Steenvoorden AC, et al. (1991). "A novel putative tyrosine kinase receptor with oncogenic potential". Oncogene 6 (11): 2113–20.  
  • Partanen J, Mäkelä TP, Alitalo R, et al. (1991). "Putative tyrosine kinases expressed in K-562 human leukemia cells". Proc. Natl. Acad. Sci. U.S.A. 87 (22): 8913–7.  
  • Neubauer A, Fiebeler A, Graham DK, et al. (1994). "Expression of axl, a transforming receptor tyrosine kinase, in normal and malignant hematopoiesis". Blood 84 (6): 1931–41.  
  • O'Bryan JP, Fridell YW, Koski R, et al. (1995). "The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage". J. Biol. Chem. 270 (2): 551–7.  
  • Lee ST, Strunk KM, Spritz RA (1993). "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes". Oncogene 8 (12): 3403–10.  
  • Schulz AS, Schleithoff L, Faust M, et al. (1993). "The genomic structure of the human UFO receptor". Oncogene 8 (2): 509–13.  
  • O'Bryan JP, Songyang Z, Cantley L, et al. (1996). "A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain". Proc. Natl. Acad. Sci. U.S.A. 93 (7): 2729–34.  
  • Mark MR, Chen J, Hammonds RG, et al. (1996). "Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl". J. Biol. Chem. 271 (16): 9785–9.  
  • Braunger J, Schleithoff L, Schulz AS, et al. (1997). "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site". Oncogene 14 (22): 2619–31.  
  • Tanaka K, Nagayama Y, Nakano T, et al. (1998). "Expression profile of receptor-type protein tyrosine kinase genes in the human thyroid". Endocrinology 139 (3): 852–8.  
  • Yanagita M, Arai H, Ishii K, et al. (2001). "Gas6 regulates mesangial cell proliferation through Axl in experimental glomerulonephritis". Am. J. Pathol. 158 (4): 1423–32.  
  • Sun WS, Misao R, Iwagaki S, et al. (2003). "Coexpression of growth arrest-specific gene 6 and receptor tyrosine kinases, Axl and Sky, in human uterine endometrium and ovarian endometriosis". Mol. Hum. Reprod. 8 (6): 552–8.  
  • D'Arcangelo D, Gaetano C, Capogrossi MC (2002). "Acidification prevents endothelial cell apoptosis by Axl activation". Circ. Res. 91 (7): e4–12.  
  • Hafizi S, Alindri F, Karlsson R, Dahlbäck B (2003). "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin". Biochem. Biophys. Res. Commun. 299 (5): 793–800.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.  
  • Ito M, Nakashima M, Nakayama T, et al. (2003). "Expression of receptor-type tyrosine kinase, Axl, and its ligand, Gas6, in pediatric thyroid carcinomas around chernobyl". Thyroid 12 (11): 971–5.  
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