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Kdel sequence     (2S)-2-[[(2S)-4-carboxy-2- [[3-carboxy-2...

Synonyms: AC1L3XJ4, 113516-56-6, Lys-asp-glu-leu, lysyl-aspartyl-glutamyl-leucine
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Disease relevance of lysyl-aspartyl-glutamyl-leucine


High impact information on lysyl-aspartyl-glutamyl-leucine


Biological context of lysyl-aspartyl-glutamyl-leucine

  • To evaluate whether E5 accumulation in the Golgi was requisite for receptor phosphorylation and cell transformation, we sequestered the E5 protein in the endoplasmic reticulum (ER)/cis Golgi by appending the ER retention KDEL sequence to its C-terminus [9].
  • Previous characterization of cDNA clones for the beta-subunit of prolyl 4-hydroxylase has indicated that its C terminus has the amino acid sequence Lys-Asp-Glu-Leu, which, it has been suggested, is necessary for the retention of a polypeptide within the lumen of the endoplasmic reticulum [10].
  • The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu) [11].
  • We have blocked CXCR4 function in CT-26 colon carcinoma cells by transfection of SDF-1, extended with a KDEL sequence [12].
  • B-fragment with a nonfunctional KDEL sequence (B-Glyc-KDELGL) was glycosylated with about the same kinetics as B-Glyc-KDEL but localized at steady state to the Golgi apparatus [13].

Anatomical context of lysyl-aspartyl-glutamyl-leucine


Associations of lysyl-aspartyl-glutamyl-leucine with other chemical compounds

  • On the contrary, the C-terminal KDEL sequence was demonstrated not to be essential for auxin binding, interaction with the plasma membrane, or activation of the transduction cascade although it does appear to be involved in the stability of ABP1 [18].
  • In this study, we observed that exogenous peptides that were artificially fused with an endoplasmic reticulum (ER) retrieval signal, a C-terminal Lys-Asp-Glu-Leu sequence, could be efficiently presented by intracellular MHC class I molecules in a TAP- and proteasome-independent, but brefeldin A-sensitive manner [19].

Gene context of lysyl-aspartyl-glutamyl-leucine

  • Total blockage of Epo secretion induced by the endoplasmic reticulum-retention amino acids Lys-Asp-Glu-Leu (KDEL) signals in 11 lines prevented autonomous proliferation, whereas a leaky retention system, observed in 3 other lines, resulted in limited autocrine stimulation without true long-term autonomous proliferation [20].
  • Calnexin (Cnx), a type-1 integral transmembrane ER protein which is partially homologous to Crt but lacks the KDEL sequence, is not detected on the cell surface either [21].
  • The surface GRP78 contains the KDEL sequence [21].
  • Surprisingly, IL-6 carrying a COOH-terminal extension of the amino acids Lys-Asp-Glu-Leu (KDEL) was not completely retained in the endoplasmic reticulum (ER) [22].
  • GFP-CRT, and GFP, with an ER signal peptide and a KDEL sequence (ER-GFP), were localised to the ER [23].

Analytical, diagnostic and therapeutic context of lysyl-aspartyl-glutamyl-leucine


  1. Function and glycosylation of plant-derived antiviral monoclonal antibody. Ko, K., Tekoah, Y., Rudd, P.M., Harvey, D.J., Dwek, R.A., Spitsin, S., Hanlon, C.A., Rupprecht, C., Dietzschold, B., Golovkin, M., Koprowski, H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. Dependence of ricin toxicity on translocation of the toxin A-chain from the endoplasmic reticulum to the cytosol. Wesche, J., Rapak, A., Olsnes, S. J. Biol. Chem. (1999) [Pubmed]
  3. Addition of an endoplasmic reticulum retrieval sequence to ricin A chain significantly increases its cytotoxicity to mammalian cells. Wales, R., Roberts, L.M., Lord, J.M. J. Biol. Chem. (1993) [Pubmed]
  4. Intracellular protein trafficking defects in human disease. Amara, J.F., Cheng, S.H., Smith, A.E. Trends Cell Biol. (1992) [Pubmed]
  5. The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. Dupuis, M., Schaerer, E., Krause, K.H., Tschopp, J. J. Exp. Med. (1993) [Pubmed]
  6. The retention signal for soluble proteins of the endoplasmic reticulum. Pelham, H.R. Trends Biochem. Sci. (1990) [Pubmed]
  7. Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells. Majoul, I.V., Bastiaens, P.I., Söling, H.D. J. Cell Biol. (1996) [Pubmed]
  8. Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. Fra, A.M., Fagioli, C., Finazzi, D., Sitia, R., Alberini, C.M. EMBO J. (1993) [Pubmed]
  9. E5 oncoprotein retained in the endoplasmic reticulum/cis Golgi still induces PDGF receptor autophosphorylation but does not transform cells. Sparkowski, J., Anders, J., Schlegel, R. EMBO J. (1995) [Pubmed]
  10. Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Helaakoski, T., Vuori, K., Myllylä, R., Kivirikko, K.I., Pihlajaniemi, T. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  11. Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C. Shorrosh, B.S., Dixon, R.A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  12. The chemokine receptor CXCR4 is required for outgrowth of colon carcinoma micrometastases. Zeelenberg, I.S., Ruuls-Van Stalle, L., Roos, E. Cancer Res. (2003) [Pubmed]
  13. Retrograde transport of KDEL-bearing B-fragment of Shiga toxin. Johannes, L., Tenza, D., Antony, C., Goud, B. J. Biol. Chem. (1997) [Pubmed]
  14. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. Yoshimori, T., Semba, T., Takemoto, H., Akagi, S., Yamamoto, A., Tashiro, Y. J. Biol. Chem. (1990) [Pubmed]
  15. Characterization of the carboxyl-terminal sequences responsible for protein retention in the endoplasmic reticulum. Andres, D.A., Rhodes, J.D., Meisel, R.L., Dixon, J.E. J. Biol. Chem. (1991) [Pubmed]
  16. C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase. Okamoto, T., Shimada, T., Hara-Nishimura, I., Nishimura, M., Minamikawa, T. Plant Physiol. (2003) [Pubmed]
  17. C-terminal KDEL-modified cystatin C is retained in transfected CHO cells. Johansen, T.E., Vogel, C.K., Schwartz, T.W. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  18. Conformational dynamics underlie the activity of the auxin-binding protein, Nt-abp1. David, K., Carnero-Diaz, E., Leblanc, N., Monestiez, M., Grosclaude, J., Perrot-Rechenmann, C. J. Biol. Chem. (2001) [Pubmed]
  19. MHC class I-associated presentation of exogenous peptides is not only enhanced but also prolonged by linking with a C-terminal Lys-Asp-Glu-Leu endoplasmic reticulum retrieval signal. Wang, L., Wu, Y.Z., Chen, A., Zhang, J.B., Yang, Z., Niu, W., Geng, M., Ni, B., Zhou, W., Zou, L.Y., Jiang, M. Eur. J. Immunol. (2004) [Pubmed]
  20. Autocrine stimulation by erythropoietin (Epo) requires Epo secretion. Villeval, J.L., Mitjavila, M.T., Dusanter-Fourt, I., Wendling, F., Mayeux, P., Vainchenker, W. Blood (1994) [Pubmed]
  21. KDEL proteins are found on the surface of NG108-15 cells. Xiao, G., Chung, T.F., Pyun, H.Y., Fine, R.E., Johnson, R.J. Brain Res. Mol. Brain Res. (1999) [Pubmed]
  22. Intracellular retention of interleukin-6 abrogates signaling. Rose-John, S., Schooltink, H., Schmitz-Van de Leur, H., Müllberg, J., Heinrich, P.C., Graeve, L. J. Biol. Chem. (1993) [Pubmed]
  23. Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors. Roderick, H.L., Campbell, A.K., Llewellyn, D.H. FEBS Lett. (1997) [Pubmed]
  24. Retention of a type II surface membrane protein in the endoplasmic reticulum by the Lys-Asp-Glu-Leu sequence. Tang, B.L., Wong, S.H., Low, S.H., Hong, W. J. Biol. Chem. (1992) [Pubmed]
  25. Retrograde transport of protein toxins under conditions of COPI dysfunction. Chen, A., Hu, T., Mikoryak, C., Draper, R.K. Biochim. Biophys. Acta (2002) [Pubmed]
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