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Gene Review

Khc  -  Kinesin heavy chain

Drosophila melanogaster

Synonyms: CG7765, DK, DKH, DmK, DmKHC, ...
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Disease relevance of Khc

  • Derivative K448-BIO contains the 448 N-terminal residues of Drosophila kinesin heavy chain fused at the C terminus to a 2-residue linker and a C-terminal fragment from Escherichia coli biotin carboxyl carrier protein; derivative K448-L is the same except that it lacks the biotin carboxyl carrier protein fragment [1].
  • The kinesin-enriched fractions were subjected to preparative SDS-PAGE, and the band representing the kinesin heavy chain was excised, homogenized, and subjected to partial enzymatic digestion with Staphylococcus aureus V8 protease [2].

Psychiatry related information on Khc


High impact information on Khc

  • The in vivo function of the microtubule motor protein kinesin was examined in Drosophila using genetics and immunolocalization [4].
  • The data indicate that kinesin function is essential and suggest that kinesin has an important role in the neuromuscular system, perhaps as a motor for axonal transport [4].
  • Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis [4].
  • The possibility of more general cellular functions remains open, but observation of embryogenesis and morphogenesis in khc mutants suggests that mitosis and the cell cycle can proceed in spite of impaired kinesin function [4].
  • Analyses of this new sequence suggest that the maximal motor unit in the kinesin superfamily may be as little as 350 amino acids, and that the existence of both kinesin and kinesin-like molecules must be an evolutionarily ancient feature of eukaryotes [5].

Biological context of Khc


Anatomical context of Khc


Associations of Khc with chemical compounds

  • Here, we show that lipid giant unilamellar vesicles (GUVs), to which kinesin molecules have been attached by means of small polystyrene beads, give rise to membrane tubes and to complex tubular networks when incubated in vitro with microtubules and ATP [12].
  • A kinesin switch I arginine to lysine mutation rescues microtubule function [13].
  • In previous work, we examined the nucleotide dependence of motility and enzymatic activity by kinesin [Shimizu, T., Furusawa, K., Ohashi, S., Toyoshima, Y. Y., Okuno, M., Malik, F., & Vale, R. D., (1991) J. Cell Biol. 112, 1189-1197] [14].
  • We investigated the kinesin stepping mechanism by immobilizing a Drosophila kinesin derivative through the carboxyl-terminal end of the neck coiled-coil domain and measuring orientations of microtubules moved by single enzyme molecules at submicromolar adenosine triphosphate concentrations [15].
  • Kinesin is a mechanochemical protein that converts the chemical energy in adenosine triphosphate into mechanical force for movement of cellular components along microtubules [16].

Physical interactions of Khc


Regulatory relationships of Khc

  • Khc mutations that reduce the velocity of kinesin-1 transport in vitro blocked streaming yet still supported posterior localization of oskar mRNA, suggesting that streaming is not essential for the oskar localization mechanism [11].

Other interactions of Khc

  • Like para and mle mutations, Khc mutations cause temperature-sensitive (TS) paralysis [20].
  • Furthermore, Khc: mutations suppress Shaker and ether-a-go-go mutations that disrupt potassium channel activity [20].
  • Furthermore, the KHC localises transiently to the posterior pole in an oskar mRNA-independent manner [7].
  • We conclude that most of the actin-rich oocyte cortex can support pole plasm assembly, and propose that Kinesin restricts pole plasm formation to the posterior by moving oskar mRNA away from microtubule-rich lateral and anterior cortical regions [21].
  • In addition, germ cells mutant for some milton or Kinesin heavy chain (Khc) alleles transport mitochondria to the oocyte prematurely and excessively, without disturbing Balbiani body-associated components [22].

Analytical, diagnostic and therapeutic context of Khc


  1. Subunit interactions in dimeric kinesin heavy chain derivatives that lack the kinesin rod. Young, E.C., Berliner, E., Mahtani, H.K., Perez-Ramirez, B., Gelles, J. J. Biol. Chem. (1995) [Pubmed]
  2. Kinesin heavy chain from bovine brain and Drosophila appear to be highly homologous molecules. Green, L.A., Kaplan, M.P., Liem, R.K. J. Neurosci. Res. (1991) [Pubmed]
  3. The C-terminal region of the stalk domain of ubiquitous human kinesin heavy chain contains the binding site for kinesin light chain. Diefenbach, R.J., Mackay, J.P., Armati, P.J., Cunningham, A.L. Biochemistry (1998) [Pubmed]
  4. Kinesin heavy chain is essential for viability and neuromuscular functions in Drosophila, but mutants show no defects in mitosis. Saxton, W.M., Hicks, J., Goldstein, L.S., Raff, E.C. Cell (1991) [Pubmed]
  5. Identification and characterization of a gene encoding a kinesin-like protein in Drosophila. McDonald, H.B., Goldstein, L.S. Cell (1990) [Pubmed]
  6. Axonal transport of mitochondria requires milton to recruit kinesin heavy chain and is light chain independent. Glater, E.E., Megeath, L.J., Stowers, R.S., Schwarz, T.L. J. Cell Biol. (2006) [Pubmed]
  7. Kinesin light chain-independent function of the Kinesin heavy chain in cytoplasmic streaming and posterior localisation in the Drosophila oocyte. Palacios, I.M., St Johnston, D. Development (2002) [Pubmed]
  8. The Drosophila kinesin-I associated protein YETI binds both kinesin subunits. Wisniewski, T.P., Tanzi, C.L., Gindhart, J.G. Biol. Cell (2003) [Pubmed]
  9. Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Hurd, D.D., Saxton, W.M. Genetics (1996) [Pubmed]
  10. Affinity purification and subcellular localization of kinesin in human neutrophils. Rothwell, S.W., Deal, C.C., Pinto, J., Wright, D.G. J. Leukoc. Biol. (1993) [Pubmed]
  11. Dynein and the actin cytoskeleton control kinesin-driven cytoplasmic streaming in Drosophila oocytes. Serbus, L.R., Cha, B.J., Theurkauf, W.E., Saxton, W.M. Development (2005) [Pubmed]
  12. A minimal system allowing tubulation with molecular motors pulling on giant liposomes. Roux, A., Cappello, G., Cartaud, J., Prost, J., Goud, B., Bassereau, P. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  13. A kinesin switch I arginine to lysine mutation rescues microtubule function. Klumpp, L.M., Mackey, A.T., Farrell, C.M., Rosenberg, J.M., Gilbert, S.P. J. Biol. Chem. (2003) [Pubmed]
  14. Comparison of the motile and enzymatic properties of two microtubule minus-end-directed motors, ncd and cytoplasmic dynein. Shimizu, T., Toyoshima, Y.Y., Edamatsu, M., Vale, R.D. Biochemistry (1995) [Pubmed]
  15. Distinguishing inchworm and hand-over-hand processive kinesin movement by neck rotation measurements. Hua, W., Chung, J., Gelles, J. Science (2002) [Pubmed]
  16. Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Yang, J.T., Saxton, W.M., Stewart, R.J., Raff, E.C., Goldstein, L.S. Science (1990) [Pubmed]
  17. Direct observation demonstrates that Liprin-alpha is required for trafficking of synaptic vesicles. Miller, K.E., DeProto, J., Kaufmann, N., Patel, B.N., Duckworth, A., Van Vactor, D. Curr. Biol. (2005) [Pubmed]
  18. A function for kinesin I in the posterior transport of oskar mRNA and Staufen protein. Brendza, R.P., Serbus, L.R., Duffy, J.B., Saxton, W.M. Science (2000) [Pubmed]
  19. Characterization of the KLP68D kinesin-like protein in Drosophila: possible roles in axonal transport. Pesavento, P.A., Stewart, R.J., Goldstein, L.S. J. Cell Biol. (1994) [Pubmed]
  20. Mutation of the axonal transport motor kinesin enhances paralytic and suppresses Shaker in Drosophila. Hurd, D.D., Stern, M., Saxton, W.M. Genetics (1996) [Pubmed]
  21. Kinesin I-dependent cortical exclusion restricts pole plasm to the oocyte posterior. Cha, B.J., Serbus, L.R., Koppetsch, B.S., Theurkauf, W.E. Nat. Cell Biol. (2002) [Pubmed]
  22. Milton controls the early acquisition of mitochondria by Drosophila oocytes. Cox, R.T., Spradling, A.C. Development (2006) [Pubmed]
  23. Decoration of the microtubule surface by one kinesin head per tubulin heterodimer. Harrison, B.C., Marchese-Ragona, S.P., Gilbert, S.P., Cheng, N., Steven, A.C., Johnson, K.A. Nature (1993) [Pubmed]
  24. Identification and partial characterization of six members of the kinesin superfamily in Drosophila. Stewart, R.J., Pesavento, P.A., Woerpel, D.N., Goldstein, L.S. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  25. Minus-end-directed motion of kinesin-coated microspheres driven by microtubule depolymerization. Lombillo, V.A., Stewart, R.J., McIntosh, J.R. Nature (1995) [Pubmed]
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