FIGURE 2 | Structure and activation of wild-type FLT3.

From the following article:

The role of FLT3 in haematopoietic malignancies

Derek L. Stirewalt & Jerald P. Radich

Nature Reviews Cancer 3, 650-665 (September 2003)

doi:10.1038/nrc1169

The role of FLT3 in haematopoietic malignancies

Transcription of the FMS-like tyrosine kinase 3 (FLT3) gene produces FLT3 mRNA, which is translated to FLT3 protein. FLT3 contains five extracellular immunoglobulin-like domains (E), a transmembrane domain (TM), a juxtamembrane domain (JM) and two tyrosine-kinase domains (K) that are linked through the tyrosine-kinase insert (KI). Cytoplasmic FLT3 undergoes glycosylation (G), which promotes localization of the receptor to the membrane. Wild-type FLT3 remains as a monomeric, inactivated protein on the cell surface until FLT3 ligand (L), probably in a dimeric form, binds the receptor and induces receptor dimerization. FLT3 dimerization promotes phosphorylation (P) of the tyrosine-kinase domains, thereby activating the receptor and downstream effectors. The dimerized receptors are quickly internalized and degraded.

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