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Kinase insert domain receptor

Introduction

Kinase insert domain receptor (KDR, a type III receptor tyrosine kinase) also known as vascular endothelial growth factor receptor 2 (VEGFR-2) is a VEGF receptor. KDR is the human gene encoding it. KDR has also been designated as CD309 (cluster of differentiation 309). KDR is also known as Flk1 (Fetal Liver Kinase 1).

The Q472H germline KDR genetic variant affects VEGFR-2 phosphorylation and has been found to associate with microvessel density in NSCLC.[1]

Interactions

Interactions

Kinase insert domain receptor has been shown to interact with SHC2,[2] Annexin A5[3] and SHC1.[4][5]

See also

See also

References

References

  1. ↑ Glubb DM, Cerri E, Giese A, Zhang W, Mirza O, Thompson EE, Chen P, Das S, Jassem J, Rzyman W, Lingen MW, Salgia R, Hirsch FR, Dziadziuszko R, Ballmer-Hofer K, Innocenti F (August 2011). “Novel functional germline variants in the VEGF receptor 2 gene and their effect on gene expression and microvessel density in lung cancer”. Clinical Cancer Research. 17 (16): 5257–67. doi:10.1158/1078-0432.CCR-11-0379. PMCΒ 3156871. PMIDΒ 21712447.
  2. ↑ Warner AJ, Lopez-Dee J, Knight EL, Feramisco JR, Prigent SA (April 2000). “The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells”. The Biochemical Journal. 347 (Pt 2): 501–9. doi:10.1042/0264-6021:3470501. PMCΒ 1220983. PMIDΒ 10749680.
  3. ↑ Wen Y, Edelman JL, Kang T, Sachs G (May 1999). “Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1”. Biochemical and Biophysical Research Communications. 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. PMIDΒ 10329451.
  4. ↑ Zanetti A, Lampugnani MG, Balconi G, Breviario F, Corada M, Lanfrancone L, Dejana E (April 2002). “Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling”. Arteriosclerosis, Thrombosis, and Vascular Biology. 22 (4): 617–22. doi:10.1161/01.ATV.0000012268.84961.AD. PMIDΒ 11950700.
  5. ↑ D’Angelo G, Martini JF, Iiri T, Fantl WJ, Martial J, Weiner RI (May 1999). “16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells”. Molecular Endocrinology. 13 (5): 692–704. doi:10.1210/mend.13.5.0280. PMIDΒ 10319320.
Further reading

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.