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Chemical Compound Review

Dilysine     (2S)-6-amino-2-[[(2S)-2,6...

Synonyms: Lysyllysine, Lys-lys, Lysyl-Lysine, L-Lys-L-lys, CHEMBL379332, ...
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Disease relevance of Dilysine


High impact information on Dilysine

  • By contrast, the dilysine retrieval signal, which competes for the same binding site on coatomer, has no effect on GTPase activity [6].
  • It is inferred that, in vivo, sorting signal selection is under kinetic control, with coatomer governing a GTPase discard pathway that excludes dilysine-tagged proteins from one class of COPI-coated vesicles [6].
  • Coatomer from beta'-COP (sec27-1) and alpha-COP (ret1-1) mutants, but not from gamma-COP (sec21) mutants, had lost the ability to bind dilysine motifs in vitro [7].
  • We describe a system to assess retrieval to the ER in yeast cells making use of a dilysine-tagged Ste2 protein [7].
  • Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum [7].

Chemical compound and disease context of Dilysine


Biological context of Dilysine


Anatomical context of Dilysine

  • Coatomer, the major component of the coat of COPI transport vesicles, binds both to the dilysine motif of resident membrane proteins of the endoplasmic reticulum and to the cytoplasmic domain of p23, a major type I membrane protein of COPI vesicles [14].
  • In the presence of dilysine, HeLa cells adhere to the apical side of epithelia and to the dorsal side of the upper layer of the blastoderm [15].
  • We used connexin constructs containing a C-terminal dilysine-based ER retention/retrieval signal (HKKSL) transfected into HeLa cells to study early events in connexin oligomerization [16].
  • Retention of BACE in the endoplasmic reticulum by introduction of a C-terminal dilysine motif prevented complex carbohydrate processing and demonstrated that propeptide cleavage occurs after exit from this organelle [17].
  • Vma21p contains a dilysine motif at the carboxy terminus, and mutation of these lysine residues abolishes retention in the endoplasmic reticulum and results in delivery of Vma21p to the vacuole, the default compartment for yeast membrane proteins [18].

Associations of Dilysine with other chemical compounds

  • Domains that contained dilysine endoplasmic reticulum retrieval signals bound the alpha-, beta'-, and epsilon-COP subunits of coatomer, whereas other p24 domains bound the beta-, gamma-, and zeta-COP subunits and required a phenylalanine-containing motif [19].
  • Significantly, production of APPbeta occurred even when APP was retained in the ER/ intermediate compartment by inhibition with brefeldin A, incubation at 15 degrees C, or by expression of exogenous APP bearing the dilysine ER retrieval motif [20].
  • Influx of glycylsarcosine and L-lysyl-L-lysine into hamster jejunum in vitro [21].
  • "Mutual" amino acid catalysis of glycine on the formation of ditryptophan, dilysine, and diserine in the prebiotically relevant Salt-Induced Peptide Formation (SIPF) Reaction was investigated varying the starting concentration and chirality of the educt amino acid, and analyzing the increase of yield resulting from this catalytic effect [22].
  • The direct superoxide scavenging ability of the tetrahydrochloride dilysine astaxanthin salt was also evaluated by electron paramagnetic resonance (EPR) spectroscopy in a well-characterized in vitro isolated human neutrophil assay [23].

Gene context of Dilysine


Analytical, diagnostic and therapeutic context of Dilysine

  • Direct titration of the apo-proteins with anions as well as anion-dependent iron release studies show that the dilysine pair is part of an active anion-binding site which exists with the Lys296-Tyr188 interaction as a core [28].
  • We now present additional evidence for this concept, based on autoaggregation studies of plastic beads coated with glycosphingolipids (GSLs) bearing Le(x) or other epitopes, and affinity chromatography on Le(x)-columns of multivalent lactofucopentaose III (Le(x) oligosaccharide) conjugated with lysyllysine [29].


  1. An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin-Darby canine kidney cells. Puertollano, R., Martínez-Menárguez, J.A., Batista, A., Ballesta, J., Alonso, M.A. Mol. Biol. Cell (2001) [Pubmed]
  2. Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site. Lontok, E., Corse, E., Machamer, C.E. J. Virol. (2004) [Pubmed]
  3. A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum. Goepfert, P.A., Shaw, K.L., Ritter, G.D., Mulligan, M.J. J. Virol. (1997) [Pubmed]
  4. Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3. Lama, J., Trono, D. J. Virol. (1998) [Pubmed]
  5. Transfected human B cells: a new model to study the functional and immunostimulatory consequences of APP production. Marx, F., Blasko, I., Zisterer, K., Grubeck-Loebenstein, B. Exp. Gerontol. (1999) [Pubmed]
  6. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Goldberg, J. Cell (2000) [Pubmed]
  7. Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum. Letourneur, F., Gaynor, E.C., Hennecke, S., Démollière, C., Duden, R., Emr, S.D., Riezman, H., Cosson, P. Cell (1994) [Pubmed]
  8. Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection. Youn, S., Collisson, E.W., Machamer, C.E. J. Virol. (2005) [Pubmed]
  9. The AP2 binding site of synaptotagmin 1 is not an internalization signal but a regulator of endocytosis. Jarousse, N., Kelly, R.B. J. Cell Biol. (2001) [Pubmed]
  10. The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants. Benghezal, M., Wasteneys, G.O., Jones, D.A. Plant Cell (2000) [Pubmed]
  11. Nonclathrin coat protein gamma, a subunit of coatomer, binds to the cytoplasmic dilysine motif of membrane proteins of the early secretory pathway. Harter, C., Pavel, J., Coccia, F., Draken, E., Wegehingel, S., Tschochner, H., Wieland, F. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  12. Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval. Andersson, H., Kappeler, F., Hauri, H.P. J. Biol. Chem. (1999) [Pubmed]
  13. Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine. Sleigh, S.H., Tame, J.R., Dodson, E.J., Wilkinson, A.J. Biochemistry (1997) [Pubmed]
  14. A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer. Harter, C., Wieland, F.T. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  15. Adhesion of malignant and nonmalignant cells to cultured embryonic substrates. de Ridder, L., Mareel, M., Vakaet, L. Cancer Res. (1975) [Pubmed]
  16. Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum. Maza, J., Das Sarma, J., Koval, M. J. Biol. Chem. (2005) [Pubmed]
  17. Maturation and endosomal targeting of beta-site amyloid precursor protein-cleaving enzyme. The Alzheimer's disease beta-secretase. Huse, J.T., Pijak, D.S., Leslie, G.J., Lee, V.M., Doms, R.W. J. Biol. Chem. (2000) [Pubmed]
  18. Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex. Hill, K.J., Stevens, T.H. Mol. Biol. Cell (1994) [Pubmed]
  19. Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Fiedler, K., Veit, M., Stamnes, M.A., Rothman, J.E. Science (1996) [Pubmed]
  20. Novel beta-secretase cleavage of beta-amyloid precursor protein in the endoplasmic reticulum/intermediate compartment of NT2N cells. Chyung, A.S., Greenberg, B.D., Cook, D.G., Doms, R.W., Lee, V.M. J. Cell Biol. (1997) [Pubmed]
  21. Influx of glycylsarcosine and L-lysyl-L-lysine into hamster jejunum in vitro. Taylor, E., Burston, D., Matthews, D.M. Clin. Sci. (1980) [Pubmed]
  22. Catalytically increased prebiotic peptide formation: ditryptophan, dilysine, and diserine. Plankensteiner, K., Reiner, H., Rode, B.M. Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life. (2005) [Pubmed]
  23. Synthesis, characterization, and direct aqueous superoxide anion scavenging of a highly water-dispersible astaxanthin-amino acid conjugate. Jackson, H.L., Cardounel, A.J., Zweier, J.L., Lockwood, S.F. Bioorg. Med. Chem. Lett. (2004) [Pubmed]
  24. New COP1-binding motifs involved in ER retrieval. Cosson, P., Lefkir, Y., Démollière, C., Letourneur, F. EMBO J. (1998) [Pubmed]
  25. RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport. Sullivan, B.M., Harrison-Lavoie, K.J., Marshansky, V., Lin, H.Y., Kehrl, J.H., Ausiello, D.A., Brown, D., Druey, K.M. Mol. Biol. Cell (2000) [Pubmed]
  26. The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. Cosson, P., Schröder-Köhne, S., Sweet, D.S., Démollière, C., Hennecke, S., Frigerio, G., Letourneur, F. Eur. J. Cell Biol. (1997) [Pubmed]
  27. The ADP-ribosylation factor GTPase-activating protein Glo3p is involved in ER retrieval. Dogic, D., de Chassey, B., Pick, E., Cassel, D., Lefkir, Y., Hennecke, S., Cosson, P., Letourneur, F. Eur. J. Cell Biol. (1999) [Pubmed]
  28. Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron-release trigger and anion-binding site. He, Q.Y., Mason, A.B., Tam, B.M., MacGillivray, R.T., Woodworth, R.C. Biochemistry (1999) [Pubmed]
  29. Further studies on cell adhesion based on Le(x)-Le(x) interaction, with new approaches: embryoglycan aggregation of F9 teratocarcinoma cells, and adhesion of various tumour cells based on Le(x) expression. Kojima, N., Fenderson, B.A., Stroud, M.R., Goldberg, R.I., Habermann, R., Toyokuni, T., Hakomori, S. Glycoconj. J. (1994) [Pubmed]
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