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  • 1
    Electronic Resource
    Electronic Resource
    Dynein binding to microtubules containing microtubule-associated proteins (1981)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1981), S. 499-515 
    Details
    ISSN: 0886-1544
    Keywords: dynein ; tubulin ; axonemes ; microtubules ; microtubule-associated proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Microtubule-associated proteins (MAPs), isolated from brain tubulin, bound to and saturated outer fibers of Chlamydomonas flagella. MAPs present on these microtubules prevented the subsequent recombination of dynein. MAPs also bound to intact axonemes and thus did not specifically bind to the dynein binding sites on the A subfiber. A molar ratio of 1 mole MAP2 per 27 moles tubulin dimers at saturation of the outer fibers with MAP2 suggested that MAPs could effectively interfere with dynein recombination only if the MAPs were near the dynein binding sites to sterically prevent binding. However, electron microscopic observations indicated that MAPs were not localized but, instead, were dispersed around the outer fibers. In addition, MAP2 present at saturating amounts on in vitro assembled brain microtubules had no significant effect on dynein binding. Dynein-decorated microtubules contained clusters of arms suggesting that there may be cooperative interaction between the arms during dynein binding. Because the A subfiber of axonemes contains sites to which dynein preferentially attaches, MAPs may prevent recombination by interfering with cooperative binding to these specific sites. Dynein presumably binds with equal affinity to any protofilament on in vitro assembled microtubules, and, therefore, the MAPs may not be capable of effectively interfering with cooperative binding of dynein to these microtubules.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970010409
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  • 2
    Electronic Resource
    Electronic Resource
    Microtubule crossbridging by Chlamydomonas dynein (1984)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 4 (1984), S. 371-385 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; dynein ; tubulin ; cilia and flagella ; microtubule associated proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Dynein, obtained from axonemes of Chlamydomonas, binds by both its A and B ends to microtubules assembled from twice cycled (2 ×) and purified (6S) brain tubulin as well as to microtubules in native spindles, thereby inducing microtubule crossbridging. The two ends of the dynein arm exhibit distinct binding characteristics for the different microtubule preparations. Greater than 99% of the dynein arms are bound exclusively by their B ends to microtubules assembled from 6S tubulin in the presence of dynein and decorated to saturation. In contrast, greater than 80% of the dynein arms are bound by both their A and B ends to and, therefore, crossbridge 6S microtubules that are only partially dynein decorated. Binding of the A end of the dynein arm to saturated 6S microtubules can be enhanced by destabilizing the binding of the B end upon addition of ATP and vanadate. These observations suggest that Chlamydomonas dynein arms can bind by their A ends to microtubules assembled from 6S tubulin only when the B ends of the arms either are not bound or are bound but do not occupy all available dynein binding sites. Dynein exhibits a slight preference for binding by its A end to microtubules assembled from 2 × tubulin and containing microtubule associated proteins (MAPs). Approximately 90% of the dynein arms crossbridge adjacent 2 × microtubles that are only partially decorated. But as saturation of these microtubules with dynein is approached, the majority of the arms are bound solely by their A ends, while a smaller percentage are bound by their B ends or by both their A and B ends. These studies indicate that the type of microtubule as well as the degree of saturation of the microtubule with dynein can determine whether microtubule crossbridging occurs.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970040506
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  • 3
    Electronic Resource
    Electronic Resource
    Interaction of chlamydomonas dynein with tubulin (1988)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 9 (1988), S. 129-139 
    Details
    ISSN: 0886-1544
    Keywords: microtubules ; motility ; cilia ; surface lattice ; biotin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Studies were conducted to determine if dynein could bind to unpolymerized tubulin. Tubulin alone normally fractionated in the included volume of a molecular sieve Bio-Gel A-1.5m column. Incubated together, tubulin and dynein coeluted in the void volumn, suggesting that a complex had formed between the two. In addition, immunoelectron microscopy revealed preassembled microtubules were labeled with biotin antibody only when incubated in both dynein and biotinylated tubulin, evidence that dynein with bound biotinylated tubulin had decorated the microtubules. A fraction of the tubulin could be dissociated from dynein by addition of ATP and vanadate, as assayed by molecular sieve chromatography followed by densitometry of gels, suggesting that some tubulin bound to the B end of the dynein arm. Additional tubulin dissociated from the dynein under conditions of high salt. These studies, together with those indicating that tubulin blocked the A end of the dynein arm from binding to microtubules and promoted the interaction of two arms at their A ends, provide evidence that the A end of the arm also can bind tubulin. Thus, the tubulin subunits, themselves, on a microtubule rather than a particular surface lattice structure formed by adjacent protofilaments may provide the binding sites for both ends of the dynein arm.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970090205
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  • 4
    Electronic Resource
    Electronic Resource
    Control of organelle transport in melanophores: Regulation of CA2+ and cAMP levels (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 22 (1992), S. 175-184 
    Details
    ISSN: 0886-1544
    Keywords: protein phosphorylation ; signal transduction ; motility ; alpha-adrenoceptors ; microtubules ; pigment ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Melanophores of the cichlid Tilapia mossambica can be induced to aggregate pigment by addition of epinephrine to the medium, suggesting adrenergic control of this transport. The melanophore response to adrenergic stimulation was examined using agonists and antagonists that are highly specific for each alpha-adrenoceptor subclass. The signal transduction mechanism of each subclass is unique: stimulation of alpha1 receptors results in a rise in intracellular free Ca2+, while alpha2 stimulation results in decreased cAMP levels [Exton, 1985: Am. J. Physiol. 248:E633-E647 ]. Each alpha1 or alpha2 specific agonist tested showed a dose dependent ability to induce aggregation and each was able to effect complete aggregation of pigment, suggesting that aggregation can be mediated either by elevating Ca2+ or by lowering cAMP. However, in the presence of either an alpha1 or an alpha2 receptor antagonist, none of the agonists were able to induce significant aggregation, suggesting that changes in levels of both messengers are required for pigment aggregation in the melanophores. Moreover, experiments in which intracellular levels of Ca2+ or cAMP were perturbed, using BAPTA and forskolin, respectively, indicated that elevating Ca2+ in the presence of high cAMP is not sufficient to induce aggregation and, conversely, that lowering cAMP levels in the presence of reduced Ca2+ is not sufficient to induce pigment aggregation. These data indicate that the concentrations of both cAMP and Ca2+ are important in regulating pigment aggregation in teleost melanophores, and suggest that maximal aggregation of pigment requires altering the levels of both messengers. © 1992 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970220305
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  • 5
    Electronic Resource
    Electronic Resource
    Cytoplasmic dynein binds to phospholipid vesicles (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 205-212 
    Details
    ISSN: 0886-1544
    Keywords: microtubule motor ; organelle transport ; vesicle transport ; liposomes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cytoplasmic dynein is the putative motor protein for retrograde organelle transport along microtubules in cells and, thus, must be capable of binding to organelle membranes. Such an attachment may occur via receptor proteins or through a direct interaction of dynein with the membrane phospholipids. We show here that cytoplasmic dynein-synaptic membrane binding does not require a receptor protein and that this binding is mediated by an electrostatic interaction with acidic phospholipids. The properties of cytoplasmic dynein binding to NaOH-extracted synaptic membranes are not significantly affected when those membranes are treated with trypsin to digest endogenous integral membrane proteins. Moreover, purified cytoplasmic dynein is capable of binding to liposomes composed of pure phospholipids. Dynein binds to liposomes with a profile remarkably similar to that of dynein binding to native membranes. Dynein-liposome binding is dependent upon the presence of acidic phospholipids and is disrupted by NaCl. Thus, these studies suggest that electrostatic interactions can effect dynein-membrane binding. © 1994 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970280304
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  • 6
    Electronic Resource
    Electronic Resource
    Ordering microtubules (1997)
    New York, NY : Wiley-Blackwell
    BioEssays 19 (1997), S. 547-550 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: How do cells order their cytoplasm? While microtubule organizing centers have long been considered essential to conferring order by virtue of their microtubule nucleating activity, attention has currently refocused on the role that microtubule motors play in organizing microtubules. An intriguing set of recent findings(1) reveals that cell fragments, lacking microtubule organizing centers, rapidly organize microtubules into a radial array during organelle transport driven by the microtubule motor, cytoplasmic dynein. Further, interaction of radial microtubules with the cell surface centers the array, revealing that centering information resides not with centrosomes but with organized microtubules.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950190704
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation of organelle transport: Lessons from color change in fish (1994)
    New York, NY : Wiley-Blackwell
    BioEssays 16 (1994), S. 727-733 
    Details
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Organelles transported along microtubules are normally moved to precise locations within cells. For example, synaptic vesiceles are transported to the neruronal synapse, the Golgi apparatus is generally found in a perinuclear location, and the membranes of the endoplasmic reticulum are actively extended to the cell periphery. The correct positioning of these organelles depends on microtubules and microtubule motors. Melanophores provide an extreme example of organized organelle transport. These cells are specialized to transport pigment granules, which are coordinately moved towards or away from the cell center, and result in the cell appearing alternately light or dark. Melanophores have proved to be an ideal system for studying the mechanisms by which the cell controls the direction of its organelle transport. Pigment granule dispersion (the movement away from the cell center) requires protein phosphorylation, while pigment aggregation (the movement towards the cell center) requires protein dephosphorylation. The target of this phosphorylation and dephosphorylation event is a protein that interacts with the microtubule motor protein, kinesin. Thus, the direction of organelle transport along microtubules may be regulated by controlling the activity of a microtubule motor.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bies.950161007
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