Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility

Vale, Ronald D.; Reese, Thomas S.; Sheetz, Michael P.

doi:10.1016/s0092-8674(85)80099-4

Cited by 1,851 publications

(1,240 citation statements)

References 40 publications

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“…Kinesin-1, the first kinesin to be discovered [79], is a tetrameric protein consisting of two identical heavy chains of Mr 120 000 and two identical light chains of Mr 64 000 (Figure 2) [80]. The mammalian genome contains three kinesin-1 heavy chain (KHC) genes (KIF5A, KIF5B and KIF5C) and three kinesin-1 light chain (KLC) genes (KLC1, KLC2, KLC3) [12].…”

Section: Kinesinmentioning

confidence: 99%

Transport and egress of herpes simplex virus in neurons

Diefenbach

Miranda-Saksena

Douglas

et al. 2007

Reviews in Medical Virology

171

150

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The mechanisms of axonal transport of the alphaherpesviruses, HSV and pseudorabies virus (PrV), in neuronal axons are of fundamental interest, particularly in comparison with other viruses, and offer potential sites for antiviral intervention or development of gene therapy vectors. These herpesviruses are transported rapidly along microtubules (MTs) in the retrograde direction from the axon terminus to the dorsal root ganglion and then anterogradely in the opposite direction. Retrograde transport follows fusion and deenvelopment of the viral capsid at the axonal membrane followed by loss of most of the tegument proteins and then binding of the capsid via one or more viral proteins (VPs) to the retrograde molecular motor dynein. The HSV capsid protein pUL35 has been shown to bind to the dynein light chain Tctex1 but is likely to be accompanied by additional dynein binding of an inner tegument protein. The mechanism of anterograde transport is much more controversial with different processes being claimed for PrV and HSV: separate transport of HSV capsid/tegument and glycoproteins versus PrV transport as an enveloped virion. The controversy has not been resolved despite application, in several laboratories, of confocal microscopy (CFM), realtime fluorescence with viruses dual labelled on capsid and glycoprotein, electron microscopy in situ and immunoelectron microscopy. Different processes for each virus seem counterintuitive although they are the most divergent in the alphaherpesvirus subfamily. Current hypotheses suggest that unenveloped HSV capsids complete assembly in the axonal growth cones and varicosities, whereas with PrV unenveloped capsids are only found travelling in a retrograde direction.

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Section: Kinesinmentioning

confidence: 99%

Transport and egress of herpes simplex virus in neurons

Diefenbach

Miranda-Saksena

Douglas

et al. 2007

Reviews in Medical Virology

171

150

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“…These results suggest that most interesting to test those dyneins that are capable of tubulin also binds to the A end of the arm, an interaction functionally rebinding to axonemes [Gibbons and Gibthat should not be dissociated by ATPhanadate. The bons, 1978;Yano and Miki-Noumura, 19811 for their observation that high-salt treatment does not usually ex-ability to promote latex bead movements [Sheetz and tract all dynein arms from axonemes is consistent with Spudich, 1983;Vale et al, 1985a-cl along in vitro-assemthe observed failure of this treatment to disrupt com-bled microtubles versus individual outer doublets. Such pletely the interaction of dynein and tubulin.…”

Section: Tubulin Promotes An Apparent Interaction Between the A Ends mentioning

confidence: 99%

Interaction of chlamydomonas dynein with tubulin

Haimo

Fenton

1988

Cell Motil. Cytoskeleton

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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.

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“…The microtubule motor protein kinesin, also known as conventional kinesin, was identified in 1985 (1,2) as the motile force underlying movement of particles along the microtubules of the giant axon of the squid. (3)(4)(5) Kinesin was shown to be capable of binding to microtubules and, in the presence of ATP, of moving towards the fast polymerizing/depolymerizing plus ends of microtubules, (6) representing the first cytoplasmic microtubule motor protein to be discovered.…”

Section: Introductionmentioning

confidence: 99%

Kinesin motors as molecular machines

Endow

2003

BioEssays

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SummaryMolecular motor proteins, fueled by energy from ATP hydrolysis, move along actin filaments or microtubules, performing work in the cell. The kinesin microtubule motors transport vesicles or organelles, assemble bipolar spindles or depolymerize microtubules, functioning in basic cellular processes. The mechanism by which motor proteins convert energy from ATP hydrolysis into work is likely to differ in basic ways from man-made machines. Several mechanical elements of the kinesin motors have now been tentatively identified, permitting researchers to begin to decipher the mechanism of motor function. The force-producing conformational changes of the motor and the means by which they are amplified are probably different for the plus-and minus-end kinesin motors.

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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility

Cited by 1,851 publications

References 40 publications

Transport and egress of herpes simplex virus in neurons

Transport and egress of herpes simplex virus in neurons

Interaction of chlamydomonas dynein with tubulin

Kinesin motors as molecular machines

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