FLT3 fusion dimers autophosphorylate

Stable Identifier
R-HSA-9703437
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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After ligand-independent dimerization, FLT3 fusion proteins are trans-autophosophorylated on tyrosine residues, activating downstream signaling through PI3K/AKT, MAP kinase and STAT5 pathways (Vu et al, 2006; Grand et al, 2007; Vu et al, 2009; Troadec et al, 2017; Chonabayashi et al, 2013; reviewed in Kazi and Roonstrand, 2019).

Literature References
PubMed ID Title Journal Year
27795560 A novel t(3;13)(q13;q12) translocation fusing FLT3 with GOLGB1: toward myeloid/lymphoid neoplasms with eosinophilia and rearrangement of FLT3?

Troadec, E, Dobbelstein, S, Bertrand, P, Faumont, N, Trimoreau, F, Touati, M, Chauzeix, J, Petit, B, Bordessoule, D, Feuillard, J, Bastard, C, Gachard, N

2017
16761019 FLT3 is fused to ETV6 in a myeloproliferative disorder with hypereosinophilia and a t(12;13)(p13;q12) translocation

Vu, HA, Xinh, PT, Masuda, M, Motoji, T, Toyoda, A, Sakaki, Y, Tokunaga, K, Sato, Y

2006
19345670 The juxtamembrane domain in ETV6/FLT3 is critical for PIM-1 up-regulation and cell proliferation

Vu, HA, Xinh, PT, Kano, Y, Tokunaga, K, Sato, Y

2009
17764812 A constitutively active SPTBN1-FLT3 fusion in atypical chronic myeloid leukemia is sensitive to tyrosine kinase inhibitors and immunotherapy

Grand, FH, Iqbal, S, Zhang, L, Russell, NH, Chase, A, Cross, NC

2007
23168613 Direct binding of Grb2 has an important role in the development of myeloproliferative disease induced by ETV6/FLT3

Chonabayashi, K, Hishizawa, M, Kawamata, S, Nagai, Y, Ohno, T, Ishikawa, T, Uchiyama, T, Takaori-Kondo, A

Leukemia 2013
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FLT3 fusion dimers [cytosol]
Physical Entity
Activity
Disease
Name Identifier Synonyms
cancer 162 malignant tumor, malignant neoplasm, primary cancer
Authored
Reviewed
Created
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