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Biochemical Society Transactions Feb 2008Dynein is an AAA+ (ATPase associated with various cellular activities)-type motor complex that utilizes ATP hydrolysis to actively drive microtubule sliding. The dynein... (Review)
Review
Dynein is an AAA+ (ATPase associated with various cellular activities)-type motor complex that utilizes ATP hydrolysis to actively drive microtubule sliding. The dynein heavy chain (molecular mass >500 kDa) contains six tandemly linked AAA+ modules and exhibits full motor activities. Detailed molecular dissection of this motor with unique architecture was hampered by the lack of an expression system for the recombinant heavy chain, as a result of its large size. However, the recent success of recombinant protein expression with full motor activities has provided a method for advances in structure-function studies in order to elucidate the molecular mechanism of force generation.
Topics: Adenosine Triphosphate; Animals; Biomechanical Phenomena; Dyneins; Metalloendopeptidases; Microtubules; Protein Structure, Tertiary
PubMed: 18208400
DOI: 10.1042/BST0360131 -
Proceedings of the National Academy of... Oct 1993Dynein is a large enzyme complex that has been found in recent years to be responsible for a variety of forms of intracellular movement associated with microtubules.... (Review)
Review
Dynein is a large enzyme complex that has been found in recent years to be responsible for a variety of forms of intracellular movement associated with microtubules. Molecular analysis of several of the polypeptide components of dynein and a related complex has provided important new insight into their structural organization and mechanism of action in the cell.
Topics: Animals; Dyneins; Macromolecular Substances; Microtubules; Models, Structural; Protein Conformation; Protein Folding
PubMed: 8415604
DOI: 10.1073/pnas.90.19.8769 -
The FEBS Journal Sep 2011The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides... (Review)
Review
The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein and myosin 5a motor proteins, with a large (and still incomplete) number of proteins involved in diverse biological functions. Despite an earlier suggestion that LC8 light chains function as cargo adapters of the above molecular motors, they are now recognized as regulatory hub proteins that interact with short linear motifs located in intrinsically disordered protein segments. The most prominent LC8 function is to promote dimerization of their binding partners that are often scaffold proteins of various complexes, including the intermediate chains of the dynein motor complex. Structural and functional aspects of this intriguing hub protein will be highlighted in this minireview.
Topics: Animals; Biological Transport; Cytoplasmic Dyneins; Cytoskeleton; Dyneins; Humans; Protein Interaction Domains and Motifs; Protein Subunits
PubMed: 21777386
DOI: 10.1111/j.1742-4658.2011.08254.x -
Cell Structure and Function Oct 1996
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European Journal of Biochemistry Apr 1990The ATPase activities in Chlamydomonas axonemes were compared between wild type and a mutant (oda) that lacks entire outer dynein arms, at various ionic strengths and pH...
The ATPase activities in Chlamydomonas axonemes were compared between wild type and a mutant (oda) that lacks entire outer dynein arms, at various ionic strengths and pH values, and in the presence of different concentrations of high-molecular-mass dextran. Over a 0-0.2 M KCl concentration range, the ATPase activity of oda axonemes was found to be 5-12 times lower than that of the wild-type axonemes. The low activity in oda is surprising since outer arm-depleted axonemes of sea urchin sperm have been reported to retain about 50% of the normal activity. In both wild type and oda, the ATPase activity of dynein was higher when contained within the axoneme than when released from it with 0.6 M KCl. The ATPase activation within the wild-type axoneme was inhibited by high ionic strengths or by the presence of dextran. The activation in oda axonemes, on the other hand, was not inhibited by these factors. These significantly different ATPase properties suggest that the inner and outer dynein arms perform somewhat different functions in this organism.
Topics: Adenosine Triphosphatases; Chlamydomonas; Dyneins; Flagella; Hydrogen-Ion Concentration; Kinetics; Mutation; Osmolar Concentration; Potassium Chloride
PubMed: 2140096
DOI: 10.1111/j.1432-1033.1990.tb15508.x -
Proceedings of the National Academy of... Feb 1981Protein carboxylmethylase (S-adenosyl-L-methionine:protein O-methyltransferase, EC 2.1.1.24.) is believed to be involved in the regulation of sperm motility. To test...
Protein carboxylmethylase (S-adenosyl-L-methionine:protein O-methyltransferase, EC 2.1.1.24.) is believed to be involved in the regulation of sperm motility. To test this hypothesis, we investigated the effects of erythro-9-[3-(2-hydroxynonyl)]adenine (EHNA) which, in combination with adenosine and homocysteine thiolactone, inhibits protein carboxylmethylase activity in monocytes. This group of compounds inhibited sea urchin sperm motility. Unexpectedly, EHNA alone inhibited the motility., This observation was confirmed in intact spermatozoa from rats, rabbits, and humans. EHNA also inhibited the motility of demembranated, reactivated sea urchin and rat spermatozoa from which protein carboxylmethylase had been extracted. In these preparations, motility was restored by ATP. These observations suggested that EHNA arrests sperm motility by inhibiting the axonemal dynein ATPase on which motility depends. Kinetic analysis demonstrated that EHNA produced mixed inhibition of both the axonemal ATPase and the partially purified dynein 1 from sea urchin sperm tails, as well as the axonemal ATPase of rat sperm tails. These observations also provide evidence for the similarity of the active site of the dynein ATPase in sea urchin and rat spermatozoa.
Topics: Adenine; Adenosine Triphosphatases; Animals; Dyneins; Humans; Immunosuppressive Agents; Kinetics; Male; Protein Methyltransferases; Protein O-Methyltransferase; Rabbits; Rats; Sea Urchins; Species Specificity; Sperm Motility; Spermatozoa
PubMed: 6453342
DOI: 10.1073/pnas.78.2.1033 -
Science Signaling Nov 2008The highly conserved DYNLL/LC8 proteins promote dimerization of a broad range of targets and are essential for the integrity, activity, or both, of many subcellular... (Review)
Review
The highly conserved DYNLL/LC8 proteins promote dimerization of a broad range of targets and are essential for the integrity, activity, or both, of many subcellular systems, such as dyneins, myosin V, and apoptotic factors. Defects in DYNLL/LC8 function lead to severe cellular and developmental phenotypes in multicellular organisms, whereas loss-of-function alleles are lethal. DYNLL/LC8 dimer formation may be controlled by various signaling inputs (including pH changes and phosphorylation), and dimerization has been linked to alterations in the enzymatic activity of neuronal nitric oxide synthase and apoptotic control. A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-kappaB.
Topics: Animals; Cytoplasmic Dyneins; Disulfides; Dyneins; Humans; NF-kappa B; Oxidation-Reduction; Transcription, Genetic
PubMed: 19036713
DOI: 10.1126/scisignal.147pe51 -
Current Opinion in Cell Biology Feb 2009Molecular motors drive key biological processes such as cell division, intracellular organelle transport, and sperm propulsion and defects in motor function can give... (Review)
Review
Molecular motors drive key biological processes such as cell division, intracellular organelle transport, and sperm propulsion and defects in motor function can give rise to various human diseases. Two dimeric microtubule-based motor proteins, kinesin-1 and cytoplasmic dynein can take over one hundred steps without detaching from the track. In this review, we discuss how these processive motors coordinate the activities of their two identical motor domains so that they can walk along microtubules.
Topics: Cell Physiological Phenomena; Dyneins; Humans; Kinesins; Microtubules; Protein Structure, Tertiary
PubMed: 19179063
DOI: 10.1016/j.ceb.2008.12.002 -
Biochemical and Biophysical Research... Apr 1978
Topics: Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Dyneins; Male; Mitosis; Myosins; Sea Urchins; Sperm Motility; Tetrahymena pyriformis; Vanadium
PubMed: 149544
DOI: 10.1016/0006-291x(78)91279-2 -
Journal of Biochemistry Aug 19791. Dynein was extracted with 0.5 M KCl from Tetrahymena axonemes. SDS-gel electrophoresis of the extract indicated that about 50% of the extracted protein had a...
1. Dynein was extracted with 0.5 M KCl from Tetrahymena axonemes. SDS-gel electrophoresis of the extract indicated that about 50% of the extracted protein had a molecular weight of about 3.5 X 10(5), and that 90% of the proteins with this weight had been extracted. 2. The ATPase [EC 3.6.1.3] reaction of the KCl-extracted dynein fraction was enhanced by 60-80% by addition of the outer doublet fraction. It showed an initial burst of Pi liberation of about 1 mol per mol of proteins with a molecular weight of 3.5 X 10(5). 3. We examined the interaction of the dynein-tubulin system from Tetrahymena cilia with ten ATP analogs [2'-dATP, 3'-dATP, epsilonATP, FTP, 8-NH(CH3)-ATP, 8,3'-S-cyclo-ATP, 8-Br-ATP, 8-OCH3-ATP, 8-SCH3-ATP, and AMPPNP]. Among them, 2'-dATP and 3'-dATP were good substrates for dynein ATPase, as they induced the dissociation of dynein arms from the B-tubule of outer doublets, the sliding movement between outer doublets, and the bending movement of axonemes. The other analogs did not induce the dissociation or the sliding movement. 4. Among the ATP analogs tested, only 2'-dATP and 3'-dATP induced the reorientation of cilia on the Triton model of Tetrahymena; the reorientation rates were smaller than that induced by ATP.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Dyneins; Kinetics; Molecular Weight; Substrate Specificity; Tetrahymena pyriformis
PubMed: 158011
DOI: 10.1093/oxfordjournals.jbchem.a132540