Importance of PTM of FLT3 in acute myeloid leukemia  

作　　者：Jianwei Liu Jianguo Gu 

机构地区：[1]Division of Regulatory Glycobiology,Institute of Molecular Biomembrane and Glycobiology,Tohoku Medical and Pharmaceutical University,4-4-1 Komatsushima,Aoba-ku,Sendai Miyagi,981-8558,Japan

出　　处：《Acta Biochimica et Biophysica Sinica》2024年第8期1199-1207,共9页生物化学与生物物理学报（英文版）

基　　金：partially supported by Grants-in-Aid for Scientific Research(23H02440 and 23K27133 to J.G.);a Grant-in-Aid for Challenging Exploratory Research(22K19443 to J.G.)from the Japan Society for the Promotion of Science(JSPS).

摘　　要：FMS-like tyrosine kinase 3(FLT3)is a receptor tyrosine kinase expressed in hematopoietic cells.Internal-tandem duplication domain(ITD)mutation and tyrosine kinase domain(TKD)mutation are the two most common mutations in acute myeloid leukemia(AML).Post-translational modifications(PTMs)of FLT3,such as glycosylation and ubiquitination,have been shown to impact various aspects of the protein in both wild-type(WT)and mutant forms of FLT3.In this review,we describe how the glycosylation status of FLT3 affects its subcellular localization,which significantly impacts the activation of downstream signaling,and the impact of specific ubiquitination on FLT3 function and stability,which may be associated with disease progression.Moreover,potential novel therapeutic strategies involving a combination of FLT3 tyrosine kinase inhibitors and drugs targeting glycosylation or ubiquitination are discussed.

关 键 词：FLT3 GLYCOSYLATION UBIQUITINATION cellular signaling AML 

分 类 号：R733.71[医药卫生—肿瘤]