Open AccessInhibition of the deubiquitinase USP10 induces degradation of SYK
Author(s) -
Jing Yang,
Chengcheng Meng,
Ellen Weisberg,
Abigail Case,
Ilaria Lamberto,
Robert S. Magin,
Sophia Adamia,
Jinhua Wang,
Nathanael S. Gray,
Suiyang Liu,
Richard Stone,
Martin Sattler,
Sara J. Buhrlage,
James D. Griffin
Publication year - 2020
Publication title -
british journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.833
H-Index - 236
eISSN - 1532-1827
pISSN - 0007-0920
DOI - 10.1038/s41416-020-0731-z
Subject(s) - syk , cancer research , deubiquitinating enzyme , tyrosine kinase , clone (java method) , myeloid leukemia , ubiquitin , fms like tyrosine kinase 3 , biology , proteasome , microbiology and biotechnology , signal transduction , gene , mutation , biochemistry
There is growing evidence that spleen tyrosine kinase (SYK) is critical for acute myeloid leukaemia (AML) transformation and maintenance of the leukemic clone in AML patients. It has also been found to be over-expressed in AML patients, with activating mutations in foetal liver tyrosine kinase 3 (FLT3), particularly those with internal tandem duplications (FLT3-ITD), where it transactivates FLT3-ITD and confers resistance to treatment with FLT3 tyrosine kinase inhibitors (TKIs).