Dimerization of KIT upon SCF binding

Stable Identifier
Reaction [binding]
Homo sapiens
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Binding of the SCF dimer to KIT rapidly triggers KIT dimerization and autophosphorylation. It is thought that one SCF dimer binds simultaneously to two KIT monomers. The fourth Ig-like domain of KIT contains the dimerisation site; deletion of this domain completely abolishes KIT dimerisation and subsequent downstream signaling (Edling et al. 2007, Blechman et al. 1995). KIT dimerization is a crucial initial step in the SCF signal transduction process.

Literature References
PubMed ID Title Journal Year
8636116 Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit

Wypych, J, Schwartz, MG, Langley, KE, Wen, J, Mendiaz, EA, Philo, JS

J Biol Chem 1996
9446650 Analysis of c-kit receptor dimerization by fluorescence resonance energy transfer

Kavanagh, TJ, Komatsu, N, Bühring, HJ, Broudy, VC, Lin, NL

Blood 1998
9045650 Kit receptor dimerization is driven by bivalent binding of stem cell factor

Schlessinger, J, Pinchasi, D, Zhou, M, Lax, I, Lemmon, MA

J Biol Chem 1997
17255936 Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases

Liu, H, Chen, X, He, X, Focia, PJ

EMBO J 2007
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