Signaling by ALK in cancer

Della Corte CM, Viscardi G, Di Liello R, Fasano M, Martinelli E, Troiani T, Ciardiello F, Morgillo F. Role and targeting of anaplastic lymphoma kinase in cancer. Molecular Cancer. 2018 Feb 19;17(1):30. doi: 10.1186/s12943-018-0776-2.; Werner MT, Zhao C, Zhang Q, Wasik MA. Nucleophosmin-anaplastic lymphoma kinase: the ultimate oncogene and therapeutic target. Blood. 2017 Feb 16;129(7):823–31. doi: 10.1182/blood-2016-05-717793. PMID: 27879258.; Hallberg B, Palmer RH. Mechanistic insight into ALK receptor tyrosine kinase in human cancer biology. Nat Rev Cancer. 2013 Oct;13(10):685–700. doi: 10.1038/nrc3580. PMID: 24060861.; Roskoski R. Anaplastic lymphoma kinase (ALK): structure, oncogenic activation, and pharmacological inhibition. Pharmacol Res. 2013 Feb;68(1):68–94. doi: 10.1016/j.phrs.2012.11.007. PMID: 23201355.; Chiarle R, Voena C, Ambrogio C, Piva R, Inghirami G. The anaplastic lymphoma kinase in the pathogenesis of cancer. Nat Rev Cancer. 2008 Jan;8(1):11–23. doi: 10.1038/nrc2291. PMID: 18097461.; Morris SW, Kirstein MN, Valentine MB, Dittmer K, Shapiro DN, Look AT, Saltman DL. Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma. Science. 1995 Jan 20;267(5196):316–7. doi: 10.1126/science.267.5196.316-b. PMID: 7824924.; Shiota M, Fujimoto J, Semba T, Satoh H, Yamamoto T, Mori S. Hyperphosphorylation of a novel 80 kDa protein-tyrosine kinase similar to Ltk in a human Ki-1 lymphoma cell line, AMS3. Oncogene. 1994 Jun;9(6):1567–74. PMID: 8183550.

Metabolites



Enzyme

EC Number name full name note
2.3.2.-
2.1.1.37 DNA (cytosine-5-)-methyltransferase S-adenosyl-L-methionine:DNA (cytosine-5-)-methyltransferase
2.1.2.3 phosphoribosylaminoimidazolecarboxamide formyltransferase 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
2.3.2.24 (E3-independent) E2 ubiquitin-conjugating enzyme S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:L-lysine ubiquitinyl transferase ([E3 ubiquitin transferase]-independent)
2.3.2.27 RING-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
2.3.2.32 cullin-RING-type E3 NEDD8 transferase [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine:[cullin] [NEDD8-protein] transferase (isopeptide bond-forming; RING-type)
2.7.1.137 phosphatidylinositol 3-kinase ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase
2.7.1.153 phosphatidylinositol-4,5-bisphosphate 3-kinase ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase
2.7.10.1 receptor protein-tyrosine kinase ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type)
2.7.10.2 non-specific protein-tyrosine kinase ATP:[protein]-L-tyrosine O-phosphotransferase (non-specific)
2.7.11.1 non-specific serine/threonine protein kinase ATP:protein phosphotransferase (non-specific)
2.7.11.24 mitogen-activated protein kinase ATP:protein phosphotransferase (MAPKK-activated)
3.1.3.16 protein-serine/threonine phosphatase protein-serine/threonine-phosphate phosphohydrolase
3.1.3.48 protein-tyrosine-phosphatase protein-tyrosine-phosphate phosphohydrolase
3.1.4.11 phosphoinositide phospholipase C 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
3.4.21.79 granzyme B
3.5.1.98 histone deacetylase histone amidohydrolase
3.5.4.10 IMP cyclohydrolase IMP 1,2-hydrolase (decyclizing)
3.6.4.13 RNA helicase
6.1.1.16 cysteine-tRNA ligase L-cysteine:tRNACys ligase (AMP-forming)


Proteins

Protein ID name full name