ZW10 Helps Recruit Dynactin and Dynein to the Kinetochore

Starr, Daniel A.; Williams, Byron; Hays, Thomas S.; Goldberg, Michael L.

doi:10.1083/jcb.142.3.763

Cited by 239 publications

(261 citation statements)

References 54 publications

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“…Although dynactin may act to increase the processivity of dynein-mediated transport (3,10), accumulating data suggest that dynactin is involved in tethering dynein to its cargo. During cell division, an interaction between the protein ZW10 and the dynamitin subunit of dynactin links dynein to the kinetochore (31). During vesicle transport, antibody inhibition of the dynein-dynactin interaction inhibits the association of dynein with membrane and therefore blocks the motility of vesicles along microtubules (6,7).…”

Section: Discussionmentioning

confidence: 99%

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

Holleran¹,

Ligon²,

Tokito³

et al. 2001

Journal of Biological Chemistry

175

160

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Cytoplasmic dynein is an intracellular motor responsible for endoplasmic reticulum-to-Golgi vesicle trafficking and retrograde axonal transport. The accessory protein dynactin has been proposed to mediate the association of dynein with vesicular cargo. Dynactin contains a 37-nm filament made up of the actin-related protein, Arp1, which may interact with a vesicle-associated spectrin network. Here, we demonstrate that Arp1 binds directly to the Golgi-associated ␤III spectrin isoform. We identify two Arp1-binding sites in ␤III spectrin, one of which overlaps with the actin-binding site conserved among spectrins. Although conventional actin binds weakly to ␤III spectrin, Arp1 binds robustly in the presence of excess F-actin. Dynein, dynactin, and ␤III spectrin co-purify on vesicles isolated from rat brain, and ␤III spectrin co-immunoprecipitates with dynactin from rat brain cytosol. In interphase cells, ␤III spectrin and dynactin both localize to cytoplasmic vesicles, co-localizing most significantly in the perinuclear region of the cell. In dividing cells, ␤III spectrin and dynactin co-localize to the developing cleavage furrow and mitotic spindle, a novel localization for ␤III spectrin. We hypothesize that the interaction between ␤III spectrin and Arp1 recruits dynein and dynactin to intracellular membranes and provides a direct link between the microtubule motor complex and its membrane-bounded cargo.The microtubule-based motor cytoplasmic dynein is involved in a wide range of cellular processes, including retrograde transport in neurons, trafficking of vesicles from the endoplasmic reticulum to the Golgi, mitotic spindle assembly, and potentially cytokinesis (reviewed in Ref. 1). These processes require the targeting of dynein to many different cellular cargoes. Whereas dynein clearly provides a motile force in all of these processes, the mechanisms linking dynein to these various cargoes have yet to be identified (reviewed in Ref. 2).Dynactin is a multi-subunit complex that binds both to microtubules (3) and to cytoplasmic dynein (4, 5). Disruption of the dynein-dynactin interaction blocks dynein-mediated transport both in vitro and in vivo (6 -9). The specific role of the interaction between dynein and dynactin is unknown. One possibility is that dynactin increases the processive nature of the movement of dynein along cellular microtubules (3, 10). A second but not mutually exclusive hypothesis is that dynactin links dynein to its cellular cargo (11).Although a dynactin-independent association between a dynein light chain and the rhodopsin receptor has been detected in rod cell vesicles (12), other studies suggest that dynactin is required to mediate the interaction of dynein with vesicular cargo. Antibodies that block the dynein-dynactin interaction deplete dynein from vesicles and inhibit microtubule-based vesicular transport (6, 7). Furthermore, disruption of the dynein-dynactin interaction by dynamitin overexpression inhibits dynein-mediated vesicle trafficking in cells (9). The nature of the interaction ...

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Section: Discussionmentioning

confidence: 99%

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

Holleran¹,

Ligon²,

Tokito³

et al. 2001

Journal of Biological Chemistry

175

160

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“…This stretching of chromatin may be due in part to the action of microtubule-based motors. The force production abilities and properties of both kinesin (Visscher et al, 1999) and dynein (Gross et al, 2000) have been shown to be modified by load, and dynein has been proposed to have a role in centromere tension leading to metaphase arrest and in chromosome motility (Starr et al, 1998;Sharp et al, 2000).…”

Section: Model For Nod Function In Meiosismentioning

confidence: 99%

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

Matthies

Baskin

Hawley

2001

MBoC

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NOD is a Drosophila chromosome-associated kinesin-like protein that does not fall into the chromokinesin subfamily. Although NOD lacks residues known to be critical for kinesin function, we show that microtubules activate the ATPase activity of NOD Ͼ2000-fold. Biochemical and genetic analysis of two genetically identified mutations of NOD (NOD DTW and NOD "DR2" ) demonstrates that this allosteric activation is critical for the function of NOD in vivo. However, several lines of evidence indicate that this ATPase activity is not coupled to vectorial transport, including 1) NOD does not produce microtubule gliding; and 2) the substitution of a single amino acid in the Drosophila kinesin heavy chain with the analogous amino acid in NOD results in a drastic inhibition of motility. We suggest that the microtubule-activated ATPase activity of NOD provides transient attachments of chromosomes to microtubules rather than producing vectorial transport.

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“…Experiments in diverse cells have demonstrated that kinesin-like proteins (KLPs) are important for mitotic spindle formation and the organized segregation of chromosomes (reviewed in Hoyt et al, 1997;Endow, 1999;Sharp et al, 2000b). Both plus-and minus-end-directed KLPs contribute to mitotic movements, and in some organisms cytoplasmic dynein is also involved (reviewed in Saunders et al, 1995;Merdes et al, 1996;Starr et al, 1998;O'Connell and Wang, 2000;Hildebrandt and Hoyt, 2000). Motors can also affect tubulin dynamics, for example, KAR3 acts to destabilize MT minus-ends (Endow et al, 1994) and XKCM1 effects general MT disassembly (Walczak et al,1996).…”

Section: Introductionmentioning

confidence: 99%

pkl1⁺andklp2⁺: Two Kinesins of the Kar3 Subfamily in Fission Yeast Perform Different Functions in Both Mitosis and Meiosis

Troxell

Sweezy

West

et al. 2001

MBoC

114

136

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We have identified Klp2p, a new kinesin-like protein (KLP) of the KAR3 subfamily in fission yeast. The motor domain of this protein is 61% identical and 71% similar to Pkl1p, another fission yeast KAR3 protein, yet the two enzymes are different in behavior and function. Pkl1p is nuclear throughout the cell cycle, whereas Klp2p is cytoplasmic during interphase. During mitosis Klp2p enters the nucleus where it forms about six chromatin-associated dots. In metaphase-arrested cells these migrate back and forth across the nucleus. During early anaphase they segregate with the chromosomes into two sets of about three, fade, and are replaced by other dots that form on the spindle interzone. Neither klp2 ϩ nor pkl1 ϩ is essential, and the double deletion is also wild type for both vegetative and sexual reproduction. Each deletion rescues different alleles of cut7 ts , a KLP that contributes to spindle formation and elongation. When either or both deletions are combined with a dynein deletion, vegetative growth is normal, but sexual reproduction fails: klp2⌬,dhc1-d1 in karyogamy, pkl1⌬,dhc1-d1 in multiple phases of meiosis, and the triple deletion in both. Deletion of Klp2p elongates a metaphase-arrested spindle, but pkl1⌬ shortens it. The anaphase spindle of klp2⌬ becomes longer than the cell, leading it to curl around the cell's ends. Apparently, Klp2p promotes spindle disassembly and contributes to the behavior of mitotic chromosomes.

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ZW10 Helps Recruit Dynactin and Dynein to the Kinetochore

Cited by 239 publications

References 54 publications

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

pkl1⁺andklp2⁺: Two Kinesins of the Kar3 Subfamily in Fission Yeast Perform Different Functions in Both Mitosis and Meiosis

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ZW10 Helps Recruit Dynactin and Dynein to the Kinetochore

Cited by 239 publications

References 54 publications

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

βIII Spectrin Binds to the Arp1 Subunit of Dynactin

Orphan Kinesin NOD Lacks Motile Properties But Does Possess a Microtubule-stimulated ATPase Activity

pkl1+andklp2+: Two Kinesins of the Kar3 Subfamily in Fission Yeast Perform Different Functions in Both Mitosis and Meiosis

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pkl1⁺andklp2⁺: Two Kinesins of the Kar3 Subfamily in Fission Yeast Perform Different Functions in Both Mitosis and Meiosis