Open Access Articles- Top Results for Megakaryocyte-associated tyrosine kinase

Megakaryocyte-associated tyrosine kinase

External IDsOMIM600038 MGI99259 HomoloGene48104 IUPHAR: 2101 ChEMBL: 4175 GeneCards: MATK Gene
EC number2.7.10.2
RNA expression pattern
File:PBB GE MATK 206267 s at tn.png
More reference expression data
RefSeq (mRNA)NM_002378NM_001285853
RefSeq (protein)NP_002369NP_001272782
Location (UCSC)Chr 19:
3.78 – 3.8 Mb
Chr 10:
81.25 – 81.26 Mb
PubMed search[1][2]

Megakaryocyte-associated tyrosine-protein kinase is an enzyme that in humans is encoded by the MATK gene.[1][2][3]

The protein encoded by this gene has amino acid sequence similarity to Csk tyrosine kinase and has the structural features of the CSK subfamily: SRC homology SH2 and SH3 domains, a catalytic domain, a unique N terminus, lack of myristylation signals, lack of a negative regulatory phosphorylation site, and lack of an autophosphorylation site. This protein is thought to play a significant role in the signal transduction of hematopoietic cells. It is able to phosphorylate and inactivate Src family kinases, and may play an inhibitory role in the control of T-cell proliferation. This protein might be involved in signaling in some cases of breast cancer. Three alternatively spliced transcript variants that encode different isoforms have been described for this gene.[3]


Megakaryocyte-associated tyrosine kinase has been shown to interact with CD117[4][5] and TrkA.[6]


  1. ^ Bennett BD, Cowley S, Jiang S, London R, Deng B, Grabarek J, Groopman JE, Goeddel DV, Avraham H (February 1994). "Identification and characterization of a novel tyrosine kinase from megakaryocytes". J Biol Chem 269 (2): 1068–74. PMID 8288563. 
  2. ^ Avraham S, Jiang S, Ota S, Fu Y, Deng B, Dowler LL, White RA, Avraham H (February 1995). "Structural and functional studies of the intracellular tyrosine kinase MATK gene and its translated product". J Biol Chem 270 (4): 1833–42. PMID 7530249. doi:10.1074/jbc.270.4.1833. 
  3. ^ a b "Entrez Gene: MATK megakaryocyte-associated tyrosine kinase". 
  4. ^ Jhun, B H; Rivnay B; Price D; Avraham H (April 1995). "The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit". J. Biol. Chem. (UNITED STATES) 270 (16): 9661–6. ISSN 0021-9258. PMID 7536744. doi:10.1074/jbc.270.16.9661. 
  5. ^ Price, D J; Rivnay B; Fu Y; Jiang S; Avraham S; Avraham H (February 1997). "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes". J. Biol. Chem. (UNITED STATES) 272 (9): 5915–20. ISSN 0021-9258. PMID 9038210. doi:10.1074/jbc.272.9.5915. 
  6. ^ Yamashita, H; Avraham S; Jiang S; Dikic I; Avraham H (May 1999). "The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells". J. Biol. Chem. (UNITED STATES) 274 (21): 15059–65. ISSN 0021-9258. PMID 10329710. doi:10.1074/jbc.274.21.15059. 

Further reading

  • Okada M, Nada S, Yamanashi Y et al. (1992). "CSK: a protein-tyrosine kinase involved in regulation of src family kinases.". J. Biol. Chem. 266 (36): 24249–52. PMID 1722201. 
  • McVicar DW, Lal BK, Lloyd A et al. (1994). "Molecular cloning of lsk, a carboxyl-terminal src kinase (csk) related gene, expressed in leukocytes.". Oncogene 9 (7): 2037–44. PMID 7516063. 
  • Jhun BH, Rivnay B, Price D, Avraham H (1995). "The MATK tyrosine kinase interacts in a specific and SH2-dependent manner with c-Kit.". J. Biol. Chem. 270 (16): 9661–6. PMID 7536744. doi:10.1074/jbc.270.16.9661. 
  • Hamaguchi I, Iwama A, Yamaguchi N et al. (1994). "Characterization of mouse non-receptor tyrosine kinase gene, HYL.". Oncogene 9 (11): 3371–4. PMID 7936664. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298. doi:10.1016/0378-1119(94)90802-8. 
  • Sakano S, Iwama A, Inazawa J et al. (1994). "Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase).". Oncogene 9 (4): 1155–61. PMID 8134117. 
  • Zrihan-Licht S, Lim J, Keydar I et al. (1997). "Association of csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells.". J. Biol. Chem. 272 (3): 1856–63. PMID 8999872. doi:10.1074/jbc.272.3.1856. 
  • Price DJ, Rivnay B, Fu Y et al. (1997). "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes.". J. Biol. Chem. 272 (9): 5915–20. PMID 9038210. doi:10.1074/jbc.272.9.5915. 
  • Hirao A, Hamaguchi I, Suda T, Yamaguchi N (1997). "Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets.". EMBO J. 16 (9): 2342–51. PMC 1169835. PMID 9171348. doi:10.1093/emboj/16.9.2342. 
  • Grgurevich S, Linnekin D, Musso T et al. (1997). "The Csk-like proteins Lsk, Hyl, and Matk represent the same Csk homologous kinase (Chk) and are regulated by stem cell factor in the megakaryoblastic cell line MO7e.". Growth Factors 14 (2-3): 103–15. PMID 9255603. doi:10.3109/08977199709021514. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149. doi:10.1016/S0378-1119(97)00411-3. 
  • Grgurevich S, Mikhael A, McVicar DW (1999). "The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells.". Biochem. Biophys. Res. Commun. 256 (3): 668–75. PMID 10080957. doi:10.1006/bbrc.1999.0398. 
  • Yamashita H, Avraham S, Jiang S et al. (1999). "The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells.". J. Biol. Chem. 274 (21): 15059–65. PMID 10329710. doi:10.1074/jbc.274.21.15059. 
  • McShan GD, Zagozdzon R, Park SY et al. (2002). "Csk homologous kinase associates with RAFTK/Pyk2 in breast cancer cells and negatively regulates its activation and breast cancer cell migration.". Int. J. Oncol. 21 (1): 197–205. PMID 12063569. doi:10.3892/ijo.21.1.197. 
  • Kim S, Zagozdzon R, Meisler A et al. (2002). "Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer.". J. Biol. Chem. 277 (39): 36465–70. PMID 12122014. doi:10.1074/jbc.M206018200. 
  • Zagozdzon R, Bougeret C, Fu Y, Avraham HK (2003). "Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells.". Int. J. Oncol. 21 (6): 1347–52. PMID 12429987. doi:10.3892/ijo.21.6.1347. 
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMC 139241. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Mikkola ET, Bergman M (2003). "Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK.". FEBS Lett. 544 (1-3): 11–4. PMID 12782282. doi:10.1016/S0014-5793(03)00405-8.