Localization of kinesin in cultured cells.

Neighbors, B; Williams, Robley C.; McIntosh, J. Richard

doi:10.1083/jcb.106.4.1193

Cited by 100 publications

(53 citation statements)

References 35 publications

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“…6B, lane 4; bottom), and found that XStau is also coimmunoprecipitated with kinesin. The SUK4 antibodies recognize conventional kinesin heavy chain (Ingold et al, 1988;Neighbors et al, 1988;Sawin et al, 1992), suggesting that the XStauassociated kinesin is kinesin I. These results indicate that XStau is associated with a kinesin motor, which may provide a mechanism for active transport of late pathway RNAs.…”

Section: Xstau Is Associated With a Kinesin Motormentioning

confidence: 62%

XenopusStaufen is a component of a ribonucleoprotein complex containing Vg1 RNA and kinesin

2004

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RNA localization is a key mechanism for generating cell and developmental polarity in a wide variety of organisms. We have performed studies to investigate a role for the Xenopus homolog of the double-stranded RNA-binding protein, Staufen, in RNA localization during oogenesis. We have found that Xenopus Staufen (XStau) is present in a ribonucleoprotein complex, and associates with both a kinesin motor protein and vegetally localized RNAs Vg1 and VegT. A functional role for XStau was revealed through expression of a dominant-negative version that blocks localization of Vg1 RNA in vivo. Our results suggest a central role for XStau in RNA localization in Xenopus oocytes, and provide evidence that Staufen is a conserved link between specific mRNAs and the RNA localization machinery.

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Section: Xstau Is Associated With a Kinesin Motormentioning

confidence: 62%

XenopusStaufen is a component of a ribonucleoprotein complex containing Vg1 RNA and kinesin

2004

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“…Consistent with this role, kinesin accumulates at nerve ligations at fast transport rates along with membranous components of axonal transport (Dahlstrom et al, 1991;Hirokawa et al, 1991;Morin et al, 1993). However, descriptions exist of kinesin immunoreactivity with a diffuse distribution (Neighbors et al, 1988) and there are suggestions that the bulk of cellular kinesin is soluble (Hollenbeck, 1989).…”

Section: Introductionmentioning

confidence: 82%

Fast axonal transport of kinesin in the rat visual system: functionality of kinesin heavy chain isoforms.

Elluru

Bloom

Brady

1995

MBoC

110

113

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The mechanochemical ATPase kinesin is thought to move membrane-bounded organelles along microtubules in fast axonal transport. However, fast transport includes several classes of organelles moving at rates that differ by an order of magnitude. Further, the fact that cytoplasmic forms of kinesin exist suggests that kinesins might move cytoplasmic structures such as the cytoskeleton. To define cellular roles for kinesin, the axonal transport of kinesin was characterized. Retinal proteins were pulse-labeled, and movement of radiolabeled kinesin through optic nerve and tract into the terminals was monitored by immunoprecipitation. Heavy and light chains of kinesin appeared in nerve and tract at times consistent with fast transport. Little or no kinesin moved with slow axonal transport indicating that effectively all axonal kinesin is associated with membranous organelles. Both kinesin heavy chain molecular weight variants of 130,000 and 124,000 Mr (KHC-A and KHC-B) moved in fast anterograde transport, but KHC-A moved at 5-6 times the rate of KHC-B. KHC-A cotransported with the synaptic vesicle marker synaptophysin, while a portion of KHC-B cotransported with the mitochondrial marker hexokinase. These results suggest that KHC-A is enriched on small tubulovesicular structures like synaptic vesicles and that at least one form of KHC-B is predominantly on mitochondria. Biochemical specialization may target kinesins to appropriate organelles and facilitate differential regulation of transport.

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“…In addition, polyclonal and monoclonal myosin antibodies have been used to inhibit the actin activated ATPase activity of myosin, (Mabuchi and Okuno, 1977;Kiehart and Pollard, 1984b;Peltz et al, 1985) to block myosin-driven motility in vitro (Kiehart and Pollard, 1984b;Flicker et al, 1985) to examine the relationship between myosin polymerization and ATPase activity as well as to probe the conformation and polymerization state of myosin (Citi and KendrickJones, 1987). Inhibitor myosin antibodies have provided evidence for the role of myosin in actin-based organelle transport (Adams and Pollard, 1986) and in cytokinesis (Mabuchi and Okuno, 1977;Kiehart et al, 1982).Kinesin antibodies have been used to establish immunological relatedness between kinesin from various cell types, as well as to identify, purify, and localize their corresponding antigens (Scholey et al, 1985;Vale et al, 1985b;Porter et al, 1987;Leslie et al, 1987;Saxton et al, 1988;Kuznetsov et al, 1988;Neighbors et al, 1988). However, none of these antikinesins was reported to inhibit kinesin activity.…”

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confidence: 99%

“…Kinesin antibodies have been used to establish immunological relatedness between kinesin from various cell types, as well as to identify, purify, and localize their corresponding antigens (Scholey et al, 1985;Vale et al, 1985b;Porter et al, 1987;Leslie et al, 1987;Saxton et al, 1988;Kuznetsov et al, 1988;Neighbors et al, 1988). However, none of these antikinesins was reported to inhibit kinesin activity.…”

mentioning

confidence: 99%

Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains.

Ingold

Cohn

Scholey

1988

The Journal of Cell Biology

174

153

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Abstract, We have prepared and characterized seven mouse monoclonal antibodies (SUK 1-7) to the 130-kD heavy chain of sea urchin egg kinesin. On immunoblots, SUK 3 and SUK 4 cross-reacted with Drosophila embryo ll6-kD heavy chains, and SUK 4, SUK 5, SUK 6, and SUK 7 bound to the 120-kD heavy chains of bovine brain kinesin. Three out of seven monoclonal antikinesins (SUK 4, SUK 6, and SUK 7) caused a dose-dependent inhibition of sea urchin egg kinesininduced microtubule translocation, whereas the other four monoclonal antibodies had no detectable effect on this motility. The inhibitory monoclonal antibodies (SUK 4, SUK 6, and SUK 7) appear to bind to spatially related sites on an ATP-sensitive microtubule binding 45-kD chymotryptic fragment of the 130-kD heavy chain, whereas SUK 2 binds to a spatially distinct site. None of the monoclonal antikinesins inhibited the microtubule activated MgATPase activity of kinesin, suggesting that SUK 4, SUK 6, and SUK 7 uncouple this MgATPase activity from motility.V ARIOUS forms of intracellular transport are thought to depend upon microtubule-associated mechanochemical ATPases (Vale, 1987). One such enzyme, kinesin (Vale et al., 1985a), binds microtubules in a nucleotide sensitive fashion, and displays a microtubule-activated ATPase activity that drives movement of kinesin-coated objects towards the plus end of microtubules (MTs) ~ in vitro (Vale et al., 1985a, b;Scholey et al., 1985;Brady, 1985; Kuznetsoy and Gelfand, 1986;Porter et al., 1987;Cohn et al., 1987;Saxton et al., 1988;Gelles et al., 1988). Kinesin from a variety of animals contains a major polypeptide with an apparent molecular mass of 110-140 kD, encoded by a single gene in Drosophila (Yang et al., 1988), plus copurifying light chains of Mr = 40-80 kD (Vale et al., 1985a,b;Amos, 1987;Kuznetsov and Gelfand, 1986;Saxton et al., 1988). Bovine brain kinesin is an tt2132 heterotetramer consisting of two 120-kD heavy chains plus two 60-kD light chains, assembled into an elongated molecule (Amos, 1987;Kuznetsov et al., 1988;Bloom et al., 1988). Kinesin is proposed to participate in organelle/vesicle transport, in organizing the endomembrane system, and in mitosis (Vale et al., 1986;Vale, 1987;Leslie et al., 1987;Schroer and Sheetz, 1988), but direct evidence concerning the biological functions of kinesin is currently lacking.Antibodies that inhibit mechanochemical activity have been extremely useful in probing the functions of myosin and 1. Abbreviations used in this paper: MT(s), microtubule(s); PMEG, 0.9 M glycerol, 0.1 M Pipes, pH 6.9, 5 mM EGTA, 2.5 mM MgSO4, 0.5 mM EDTA, 1 mM DTT, 100 Ixg/ml soybean trypsin inhibitor, 1 mg/mlp-tosyl-Larginine methyl ester hydrochloride, 10 Ixg/ml leupeptin, pepstatin, and aprotinin; RT, room temperature. dynein. For example, an antiserum that inhibits the ATPase activity of sea urchin sperm dynein caused a corresponding decrease in the beat frequency of reactivated sea urchin sperm, supporting the hypothesis that the dynein ATPase drives axonemal motility (Ogawa and Mohri, 1975;O...

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Localization of kinesin in cultured cells.

Cited by 100 publications

References 35 publications

XenopusStaufen is a component of a ribonucleoprotein complex containing Vg1 RNA and kinesin

XenopusStaufen is a component of a ribonucleoprotein complex containing Vg1 RNA and kinesin

Fast axonal transport of kinesin in the rat visual system: functionality of kinesin heavy chain isoforms.

Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains.

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