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DNAH8  -  dynein, axonemal, heavy chain 8

Homo sapiens

Synonyms: ATPase, Axonemal beta dynein heavy chain 8, Ciliary dynein heavy chain 8, Dynein heavy chain 8, axonemal, hdhc9
 
 
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Disease relevance of DNAH8

  • The putative proteasome-associated proteins Mpa (Mycobaterium proteasomal ATPase) and PafA (proteasome accessory factor A) of the human pathogen Mycobacterium tuberculosis (Mtb) are essential for virulence and resistance to nitric oxide [1].
  • Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity [2].
  • Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure [3].
  • The possible significance of the observed differences between the myosin Mg2+ ATPase activation by chronic lymphocytic leukemia and normal lymphocyte actin is discussed [4].
  • Consistent with a previous report that identifies an equivalent mutation in a copper-transporting P(1B)-type ATPase of a Wilson disease patient, the PCA1 allele found in laboratory yeast strains is nonfunctional [5].
 

Psychiatry related information on DNAH8

  • We demonstrate that the insertion of the B2 sequence reduces the motor activity of Dictyostelium myosin II, with reduction of the maximal actin-activated ATPase activity and a decrease in the affinity for actin [6].
  • Sodium-potassium/ATPase is of paramount importance for the proper functioning of the brain and its involvement in the affective disorders has been claimed for a long time [7].
  • A time response study showed an increase in the activity of the Na(+)-K(+) ATPase in the left and right ventricles of animals treated with the cytokine, with no change in its protein expression [8].
  • The aim of this work was to determine if electroconvulsive shock (ECS) would induce changes in the high-affinity binding of ouabain to the sodium-potassium/ATPase from rat brain regions [7].
 

High impact information on DNAH8

  • Tilting of the light-chain domain of the head with respect to its actin-bound catalytic domain is thought to be coupled to the ATPase cycle [9].
  • Myosin, the ATPase that interacts with actin to produce the force for muscle contraction and other forms of cell motility, is believed to be involved in cytokinesis but not in mitosis [10].
  • Gle1 and the phosphoinositide IP6 activate Dbp5's ATPase activity in vitro and this could provide critical spatial regulation of Dbp5 activity in vivo [11].
  • A random hydrolysis mechanism is ruled out by the observed inhibition of ATPase in a mixed hexamer containing wt and an inactive Rho mutant [12].
  • Cdc48 (p97), a conserved chaperone-like ATPase of eukaryotic cells, has attracted attention recently because of its wide range of cellular functions [13].
 

Chemical compound and disease context of DNAH8

 

Biological context of DNAH8

  • The steady-state actin-activated ATPase of phosphorylated filaments was 30-100-fold higher than that of antibody-stabilized dephosphorylated filaments, suggesting that phosphorylation can activate ATPase activity independent of changes in assembly [19].
  • Here we report that SNF2H, the mammalian ISWI chromatin remodeling ATPase, is critical for repression of a genomically integrated, TR-regulated reporter gene [20].
  • Effect of lysine methylation and other ATPase modulators on the active site of myosin subfragment 1 [21].
  • While the SecA ATPase drives protein translocation across the bacterial cytoplasmic membrane by interacting with the SecYEG translocon, molecular details of SecA-SecY interaction remain poorly understood [22].
  • Differences between the alternative exons presumably determine the lower ATPase activity of smooth muscle myosin, contribute to the different structure of the striated and smooth muscle thick filaments, and may also be important for the molecular mechanism of the catch phenomenon [23].
 

Anatomical context of DNAH8

  • Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain [24].
  • A fraction has been obtained from baby hamster kidney (BHK-21) cells that will stimulate the actin-moderated ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity of both BHK-21 myosin and gizzard smooth muscle myosin [25].
  • Stringent proteomic and two-hybrid analyses show that Spp382p also interacts with Cwc23p, a DNA J-like protein present in the spliceosome and copurified with the Prp43p DExD/H-box ATPase [26].
  • Myofibrillar but not actomyosin ATPase is depressed in failing myocardium from patients with dilated cardiomyopathy [3].
  • The Vmax of the actin-activated myosin Mg2+ ATPase activity was compared using rabbit skeletal muscle heavy meromyosin and subfragment 1 preparations [4].
 

Associations of DNAH8 with chemical compounds

  • Bafilomycin A1, an inhibitor of the vacuolar ATPase proton pump, completely prevented EF activity, even when added long after the toxin [27].
  • Removal of the last 11 residues (residues 243-253) from cyto-EpsL prevented cardiolipin binding as well as stimulation of the ATPase activity of EpsE [28].
  • Our results indicate that caspase-3 cleaved myofibrillar proteins, resulting in an impaired force/Ca(2+) relationship and myofibrillar ATPase activity [29].
  • To test whether dimerization per se restores regulation of ATPase activity, mutants were expressed with varying lengths of rod sequence, followed by C-terminal leucine zippers to stabilize the coiled-coil [30].
  • Interaction with ArsD increases the affinity of ArsA for arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion [31].
 

Analytical, diagnostic and therapeutic context of DNAH8

  • We report X-ray solution scattering and electron microscopy structures of the activated, full-length nitrogen-regulatory protein C (NtrC) showing a novel mechanism for regulation of AAA+ ATPase assembly via the juxtaposition of the receiver domains and ATPase ring [32].
  • Finally, recent biochemical dissection of the ATPase cycle and its coupling to protein unfolding has revealed fundamental operating principles of this important, ubiquitous family of molecular machines [33].
  • Indeed, axoplasm contains actin-dependent ATPase activity, and a pan-myosin antibody recognized at least four bands in Western blots of axoplasm [34].
  • Immobilization has produced a decrease more than threefold in gene expression of enzymes involved in energy metabolism, especially ATPase, cytochrome c oxidase, NADH dehydrogenase, and protein phosphatase 1 [35].
  • Site-directed mutagenesis was used to probe the relationship between the structure of the gamma regulatory segment and its function in ATPase regulation via its interaction with the inhibitory epsilon subunit [36].

References

  1. Identification of substrates of the Mycobacterium tuberculosis proteasome. Pearce, M.J., Arora, P., Festa, R.A., Butler-Wu, S.M., Gokhale, R.S., Darwin, K.H. EMBO J. (2006) [Pubmed]
  2. Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity. Schlief, M.L., West, T., Craig, A.M., Holtzman, D.M., Gitlin, J.D. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure. Nguyen, T.T., Hayes, E., Mulieri, L.A., Leavitt, B.J., ter Keurs, H.E., Alpert, N.R., Warshaw, D.M. Circ. Res. (1996) [Pubmed]
  4. Purification and characterization of actin from normal and chronic lymphocytic leukemia lymphocytes. Liebes, L.F., Stark, R., Nevrla, D., Grusky, G., Zucker-Franklin, D., Silber, R. Cancer Res. (1983) [Pubmed]
  5. A Cadmium-transporting P1B-type ATPase in Yeast Saccharomyces cerevisiae. Adle, D.J., Sinani, D., Kim, H., Lee, J. J. Biol. Chem. (2007) [Pubmed]
  6. Functional characterization of vertebrate nonmuscle myosin IIB isoforms using Dictyostelium chimeric myosin II. Takahashi, M., Takahashi, K., Hiratsuka, Y., Uchida, K., Yamagishi, A., Uyeda, T.Q., Yazawa, M. J. Biol. Chem. (2001) [Pubmed]
  7. Repeated electroconvulsive shock induces changes in high-affinity [3H]-ouabain binding to rat striatal membranes. Bignotto, M., Benedito, M.A. Neurochem. Res. (2006) [Pubmed]
  8. Tumor necrosis factor alpha alters Na(+)-K(+) ATPase activity in rat cardiac myocytes: Involvement of NF-kappaB, AP-1 and PGE(2). Skayian, Y., Kreydiyyeh, S.I. Life Sci. (2006) [Pubmed]
  9. Elastic bending and active tilting of myosin heads during muscle contraction. Dobbie, I., Linari, M., Piazzesi, G., Reconditi, M., Koubassova, N., Ferenczi, M.A., Lombardi, V., Irving, M. Nature (1998) [Pubmed]
  10. Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle. Scholey, J.M., Porter, M.E., Grissom, P.M., McIntosh, J.R. Nature (1985) [Pubmed]
  11. Transport of messenger RNA from the nucleus to the cytoplasm. Cole, C.N., Scarcelli, J.J. Curr. Opin. Cell Biol. (2006) [Pubmed]
  12. Mechanochemistry of transcription termination factor Rho. Adelman, J.L., Jeong, Y.J., Liao, J.C., Patel, G., Kim, D.E., Oster, G., Patel, S.S. Mol. Cell (2006) [Pubmed]
  13. Cdc48 (p97): a 'molecular gearbox' in the ubiquitin pathway? Jentsch, S., Rumpf, S. Trends Biochem. Sci. (2007) [Pubmed]
  14. Bafilomycin Induces the p21-Mediated Growth Inhibition of Cancer Cells under Hypoxic Conditions by Expressing Hypoxia-Inducible Factor-1{alpha}. Lim, J.H., Park, J.W., Kim, M.S., Park, S.K., Johnson, R.S., Chun, Y.S. Mol. Pharmacol. (2006) [Pubmed]
  15. Autosomal-dominant calcium ATPase disorders. Szigeti, R., Kellermayer, R. J. Invest. Dermatol. (2006) [Pubmed]
  16. Pseudomonas aeruginosa pyocyanin inactivates lung epithelial vacuolar ATPase-dependent cystic fibrosis transmembrane conductance regulator expression and localization. Kong, F., Young, L., Chen, Y., Ran, H., Meyers, M., Joseph, P., Cho, Y.H., Hassett, D.J., Lau, G.W. Cell. Microbiol. (2006) [Pubmed]
  17. Abnormalities of Na/K ATPase in migraine with aura. Scarrone, S., Podestà, M., Cupello, A., Finocchi, C., Frassoni, F., Gandolfo, C., Balestrino, M. Cephalalgia : an international journal of headache (2007) [Pubmed]
  18. A peptide inhibitor of MurA UDP-N-acetylglucosamine enolpyruvyl transferase: The first committed step in peptidoglycan biosynthesis. Molina-L??pez, J., Sanschagrin, F., Levesque, R.C. Peptides (2006) [Pubmed]
  19. Filamentous smooth muscle myosin is regulated by phosphorylation. Trybus, K.M. J. Cell Biol. (1989) [Pubmed]
  20. The N-CoR complex enables chromatin remodeler SNF2H to enhance repression by thyroid hormone receptor. Alenghat, T., Yu, J., Lazar, M.A. EMBO J. (2006) [Pubmed]
  21. Effect of lysine methylation and other ATPase modulators on the active site of myosin subfragment 1. Bivin, D.B., Ue, K., Khoroshev, M., Morales, M. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  22. Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking. Mori, H., Ito, K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  23. Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene. Nyitray, L., Jancsó, A., Ochiai, Y., Gráf, L., Szent-Györgyi, A.G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  24. Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain. Trybus, K.M., Waller, G.S., Chatman, T.A. J. Cell Biol. (1994) [Pubmed]
  25. Calcium-sensitive regulation of actin-myosin interactions in baby hamster kidney (BHK-21) cells. Yerna, M.J., Dabrowska, R., Hartshorne, D.J., Goldman, R.D. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  26. Inhibition of a spliceosome turnover pathway suppresses splicing defects. Pandit, S., Lynn, B., Rymond, B.C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  27. Cell entry and cAMP imaging of anthrax edema toxin. Dal Molin, F., Tonello, F., Ladant, D., Zornetta, I., Zamparo, I., Di Benedetto, G., Zaccolo, M., Montecucco, C. EMBO J. (2006) [Pubmed]
  28. Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids. Camberg, J.L., Johnson, T.L., Patrick, M., Abendroth, J., Hol, W.G., Sandkvist, M. EMBO J. (2007) [Pubmed]
  29. Functional consequences of caspase activation in cardiac myocytes. Communal, C., Sumandea, M., de Tombe, P., Narula, J., Solaro, R.J., Hajjar, R.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  30. Spare the rod, spoil the regulation: necessity for a myosin rod. Trybus, K.M., Freyzon, Y., Faust, L.Z., Sweeney, H.L. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  31. An arsenic metallochaperone for an arsenic detoxification pump. Lin, Y.F., Walmsley, A.R., Rosen, B.P. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  32. The structural basis for regulated assembly and function of the transcriptional activator NtrC. De Carlo, S., Chen, B., Hoover, T.R., Kondrashkina, E., Nogales, E., Nixon, B.T. Genes Dev. (2006) [Pubmed]
  33. ATP-dependent proteases of bacteria: recognition logic and operating principles. Baker, T.A., Sauer, R.T. Trends Biochem. Sci. (2006) [Pubmed]
  34. Evidence for myosin motors on organelles in squid axoplasm. Bearer, E.L., DeGiorgis, J.A., Bodner, R.A., Kao, A.W., Reese, T.S. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  35. Characterization of control and immobilized skeletal muscle: an overview from genetic engineering. St-Amand, J., Okamura, K., Matsumoto, K., Shimizu, S., Sogawa, Y. FASEB J. (2001) [Pubmed]
  36. Structural Analysis of the Regulatory Dithiol-containing Domain of the Chloroplast ATP Synthase {gamma} Subunit. Samra, H.S., Gao, F., He, F., Hoang, E., Chen, Z., Gegenheimer, P.A., Berrie, C.L., Richter, M.L. J. Biol. Chem. (2006) [Pubmed]
 
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