Phospho-eEF2K (S359) Polyclonal Antibody, 100µg, (ATB-P1093)

Description

Background:

This gene encodes a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links activation of cell surface receptors to cell division. This kinase is involved in the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function. The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment. [provided by RefSeq, Jul 2008]

Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.

Product datasheet:

References:

1. Eukaryotic elongation factor 2 kinase activity is controlled by multiple inputs from oncogenic signaling. Wang X, et al. Mol Cell Biol, 2014 Nov 15. PMID 25182533
2. The molecular mechanism of eukaryotic elongation factor 2 kinase activation. Tavares CD, et al. J Biol Chem, 2014 Aug 22. PMID 25012662
3. A conserved loop in the catalytic domain of eukaryotic elongation factor 2 kinase plays a key role in its substrate specificity. Moore CE, et al. Mol Cell Biol, 2014 Jun. PMID 24732796 Free PMC Article
4. Targeting elongation factor-2 kinase (eEF-2K) induces apoptosis in human pancreatic cancer cells. Ashour AA, et al. Apoptosis, 2014 Jan. PMID 24193916
5. Roles of eEF-2 kinase in cancer. Liu XY, et al. Chin Med J (Engl), 2012 Aug. PMID 22932089
6. Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase.
   Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V., Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G., Prostko C.R., Germino F.J., Hait W.N.
   Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANT ARG-361. Tissue: Glial tumor.
7. The sequence and analysis of duplication-rich human chromosome 16.
   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
   , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
   Nature 432:988-994(2004) [PubMed] [Europe PMC]

   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

8. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-23 AND ARG-361. Tissue: Lymph.
9. Mapping the functional domains of elongation factor-2 kinase.
   Pavur K.S., Petrov A.N., Ryazanov A.G.
   Biochemistry 39:12216-12224(2000) [PubMed] [Europe PMC] Cited for: AUTOPHOSPHORYLATION, DOMAIN.
10. A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta.
    Knebel A., Morrice N., Cohen P.
    EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION AT SER-359.