FLT4
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| Fms-srodna tirozinska kinaza 4 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Dostupne strukture | |||||||||||
| 4BSJ, 4BSK | |||||||||||
| Identifikatori | |||||||||||
| Simboli | FLT4; FLT41; LMPH1A; PCL; VEGFR3 | ||||||||||
| Vanjski ID | OMIM: 136352 MGI: 95561 HomoloGene: 7321 GeneCards: FLT4 Gene | ||||||||||
| EC broj | 2.7.10.1 | ||||||||||
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| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 2324 | 14257 | |||||||||
| Ensembl | ENSG00000037280 | ENSMUSG00000020357 | |||||||||
| UniProt | P35916 | P35917 | |||||||||
| Ref. Sekv. (iRNK) | NM_002020 | NM_008029 | |||||||||
| Ref. Sekv. (protein) | NP_002011 | NP_032055 | |||||||||
| Lokacija (UCSC) | Chr 5: 180.03 - 180.08 Mb | Chr 11: 49.61 - 49.65 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
Fms-srodna tirozinska kinaza 4, takođe poznata kao FLT4, protein je koji je kod ljudi kodiran FLT4 genom.[1][2]
Ovaj gen kodira receptor tirozinske kinaze za vaskularne endotelne faktore rasta C i D. Smatra se da ovaj protein učestvuje u limfangiogenezi i održavanju limfhatičnog endotela. Mutacije ovog gena uzrokuju nasledni lomfedem tipa IA.[1]
FLT4 formira interakcije sa SHC1.[3][4][5]
- ↑ 1,0 1,1 „Entrez Gene: FLT4 fms-related tyrosine kinase 4”.
- ↑ Galland F, Karamysheva A, Mattei MG, Rosnet O, Marchetto S, Birnbaum D (June 1992). „Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene”. Genomics 13 (2): 475–8. DOI:10.1016/0888-7543(92)90277-Y. PMID 1319394.
- ↑ Pajusola, K; Aprelikova O; Pelicci G; Weich H; Claesson-Welsh L; Alitalo K (December 1994). „Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors”. Oncogene (ENGLAND) 9 (12): 3545–55. ISSN 0950-9232. PMID 7970715.
- ↑ Fournier, E; Blaikie P; Rosnet O; Margolis B; Birnbaum D; Borg J P (January 1999). „Role of tyrosine residues and protein interaction domains of SHC adaptor in VEGF receptor 3 signaling”. Oncogene (ENGLAND) 18 (2): 507–14. DOI:10.1038/sj.onc.1202315. ISSN 0950-9232. PMID 9927207.
- ↑ Fournier, E; Rosnet O; Marchetto S; Turck C W; Rottapel R; Pelicci P G; Birnbaum D; Borg J P (May 1996). „Interaction with the phosphotyrosine binding domain/phosphotyrosine interacting domain of SHC is required for the transforming activity of the FLT4/VEGFR3 receptor tyrosine kinase”. J. Biol. Chem. (UNITED STATES) 271 (22): 12956–63. DOI:10.1074/jbc.271.22.12956. ISSN 0021-9258. PMID 8662748.
- Petrova TV, Makinen T, Alitalo K (1999). „Signaling via vascular endothelial growth factor receptors.”. Exp. Cell Res. 253 (1): 117–30. DOI:10.1006/excr.1999.4707. PMID 10579917.
- Aprelikova O, Pajusola K, Partanen J, et al. (1992). „FLT4, a novel class III receptor tyrosine kinase in chromosome 5q33-qter.”. Cancer Res. 52 (3): 746–8. PMID 1310071.
- Galland F, Karamysheva A, Mattei MG, et al. (1992). „Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene.”. Genomics 13 (2): 475–8. DOI:10.1016/0888-7543(92)90277-Y. PMID 1319394.
- Pajusola K, Aprelikova O, Korhonen J, et al. (1992). „FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines.”. Cancer Res. 52 (20): 5738–43. PMID 1327515.
- Fournier E, Dubreuil P, Birnbaum D, Borg JP (1995). „Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor.”. Oncogene 11 (5): 921–31. PMID 7675451.
- Pajusola K, Aprelikova O, Armstrong E, et al. (1993). „Two human FLT4 receptor tyrosine kinase isoforms with distinct carboxy terminal tails are produced by alternative processing of primary transcripts.”. Oncogene 8 (11): 2931–7. PMID 7692369.
- Pajusola K, Aprelikova O, Pelicci G, et al. (1994). „Signalling properties of FLT4, a proteolytically processed receptor tyrosine kinase related to two VEGF receptors.”. Oncogene 9 (12): 3545–55. PMID 7970715.
- Galland F, Karamysheva A, Pebusque MJ, et al. (1993). „The FLT4 gene encodes a transmembrane tyrosine kinase related to the vascular endothelial growth factor receptor.”. Oncogene 8 (5): 1233–40. PMID 8386825.
- Fournier E, Rosnet O, Marchetto S, et al. (1996). „Interaction with the phosphotyrosine binding domain/phosphotyrosine interacting domain of SHC is required for the transforming activity of the FLT4/VEGFR3 receptor tyrosine kinase.”. J. Biol. Chem. 271 (22): 12956–63. DOI:10.1074/jbc.271.22.12956. PMID 8662748.
- Lee J, Gray A, Yuan J, et al. (1996). „Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4.”. Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1988–92. DOI:10.1073/pnas.93.5.1988. PMC 39896. PMID 8700872.
- Kukk E, Lymboussaki A, Taira S, et al. (1997). „VEGF-C receptor binding and pattern of expression with VEGFR-3 suggests a role in lymphatic vascular development.”. Development 122 (12): 3829–37. PMID 9012504.
- Achen MG, Jeltsch M, Kukk E, et al. (1998). „Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4).”. Proc. Natl. Acad. Sci. U.S.A. 95 (2): 548–53. DOI:10.1073/pnas.95.2.548. PMC 18457. PMID 9435229.
- Ferrell RE, Levinson KL, Esman JH, et al. (1999). „Hereditary lymphedema: evidence for linkage and genetic heterogeneity.”. Hum. Mol. Genet. 7 (13): 2073–8. DOI:10.1093/hmg/7.13.2073. PMID 9817924.
- Fournier E, Blaikie P, Rosnet O, et al. (1999). „Role of tyrosine residues and protein interaction domains of SHC adaptor in VEGF receptor 3 signaling.”. Oncogene 18 (2): 507–14. DOI:10.1038/sj.onc.1202315. PMID 9927207.
- Karkkainen MJ, Ferrell RE, Lawrence EC, et al. (2000). „Missense mutations interfere with VEGFR-3 signalling in primary lymphoedema.”. Nat. Genet. 25 (2): 153–9. DOI:10.1038/75997. PMID 10835628.
- Irrthum A, Karkkainen MJ, Devriendt K, et al. (2000). „Congenital hereditary lymphedema caused by a mutation that inactivates VEGFR3 tyrosine kinase.”. Am. J. Hum. Genet. 67 (2): 295–301. DOI:10.1086/303019. PMC 1287178. PMID 10856194.
- Wang JF, Zhang XF, Groopman JE (2001). „Stimulation of beta 1 integrin induces tyrosine phosphorylation of vascular endothelial growth factor receptor-3 and modulates cell migration.”. J. Biol. Chem. 276 (45): 41950–7. DOI:10.1074/jbc.M101370200. PMID 11553610.
- Baldwin ME, Roufail S, Halford MM, et al. (2001). „Multiple forms of mouse vascular endothelial growth factor-D are generated by RNA splicing and proteolysis.”. J. Biol. Chem. 276 (47): 44307–14. DOI:10.1074/jbc.M106188200. PMID 11574540.
- Walter JW, North PE, Waner M, et al. (2002). „Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma.”. Genes Chromosomes Cancer 33 (3): 295–303. DOI:10.1002/gcc.10028. PMID 11807987.