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Gene Review

MELK  -  maternal embryonic leucine zipper kinase

Homo sapiens

Synonyms: KIAA0175, Maternal embryonic leucine zipper kinase, Protein kinase Eg3, Protein kinase PK38, Tyrosine-protein kinase MELK, ...
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Disease relevance of MELK


High impact information on MELK

  • Here we demonstrate that LKB1 can phosphorylate the T-loop of all the members of this subfamily, apart from MELK, increasing their activity >50-fold [3].
  • Although MELK has been implicated in regulating the cell cycle, our data suggest that PIG-1, like other PAR-1 family members, regulates cell polarity [4].
  • We show here that MELK has a rather broad substrate specificity and does not appear to require a specific sequence surrounding its (auto)phosphorylation sites [5].
  • The smallest MELK fragment that was still catalytically active comprises the N-terminal catalytic domain and the flanking ubiquitin-associated domain [5].
  • We have mapped no less than 16 autophosphorylation sites including serines, threonines, and a tyrosine residue and show that the phosphorylation of Thr167 and Ser171 is required for the activation of MELK [5].

Biological context of MELK


Anatomical context of MELK

  • Recombinant MELK was a potent inhibitor of an early step of spliceosome assembly in nuclear extracts [6].
  • RESULTS : Northern blot analyses on multiple human tissues and cancer cell lines demonstrated that MELK was overexpressed at a significantly high level in a great majority of breast cancers and cell lines, but was not expressed in normal vital organs (heart, liver, lung and kidney) [1].

Associations of MELK with chemical compounds


Other interactions of MELK

  • Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1 [6].

Analytical, diagnostic and therapeutic context of MELK

  • Interlocking MELK with the drug screening machinery provides new clues related to the selection of target proteins, and functionally relevant hits and drug leads [7].


  1. Involvement of maternal embryonic leucine zipper kinase (MELK) in mammary carcinogenesis through interaction with Bcl-G, a pro-apoptotic member of the Bcl-2 family. Lin, M.L., Park, J.H., Nishidate, T., Nakamura, Y., Katagiri, T. Breast Cancer Res. (2007) [Pubmed]
  2. Effect of low lactose milk Eiwit Melk (E.M.) on protein calorie malnutrition. Suharjono, n.u.l.l., Wirya, W., Samsudin, n.u.l.l., Sunoto, n.u.l.l., Sulaiman, Z., Sutedjo, n.u.l.l. Paediatrica Indonesiana. (1975) [Pubmed]
  3. LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. Lizcano, J.M., Göransson, O., Toth, R., Deak, M., Morrice, N.A., Boudeau, J., Hawley, S.A., Udd, L., Mäkelä, T.P., Hardie, D.G., Alessi, D.R. EMBO J. (2004) [Pubmed]
  4. The C. elegans MELK ortholog PIG-1 regulates cell size asymmetry and daughter cell fate in asymmetric neuroblast divisions. Cordes, S., Frank, C.A., Garriga, G. Development (2006) [Pubmed]
  5. Substrate specificity and activity regulation of protein kinase MELK. Beullens, M., Vancauwenbergh, S., Morrice, N., Derua, R., Ceulemans, H., Waelkens, E., Bollen, M. J. Biol. Chem. (2005) [Pubmed]
  6. Inhibition of spliceosome assembly by the cell cycle-regulated protein kinase MELK and involvement of splicing factor NIPP1. Vulsteke, V., Beullens, M., Boudrez, A., Keppens, S., Van Eynde, A., Rider, M.H., Stalmans, W., Bollen, M. J. Biol. Chem. (2004) [Pubmed]
  7. Topological proteomics, toponomics, MELK-technology. Schubert, W. Adv. Biochem. Eng. Biotechnol. (2003) [Pubmed]
  8. Effect of low lactose milk "Eiwit Melk" (E.M.) on low birth weight infants with diarrhoea. Bagdadiji, T., Suharjono, n.u.l.l., Boediarso, A., Sunoto, n.u.l.l. Paediatrica Indonesiana. (1975) [Pubmed]
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