Myosin II Is Involved in the Production of Constitutive Transport Vesicles from the TGN

Müsch, Anne; Cohen, David; Rodríguez-Boulan, Enrique

doi:10.1083/jcb.138.2.291

Cited by 171 publications

(152 citation statements)

References 78 publications

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“…Kinesins are known to transport vesicular cargo, and roles of membrane insertion during cytokinesis and deposition of special lipids in the region of the cleavage furrow have been documented recently (34,35). Thus, this simplest model of Kif12-driven myosin translocation could be vesicle-mediated, with the vesicles being inserted into the cleavage furrow membrane during furrow formation (36). …”

Section: Discussionmentioning

confidence: 99%

A mitotic kinesin-like protein required for normal karyokinesis, myosin localization to the furrow, and cytokinesis in Dictyostelium

Lakshmikanth

Warrick²,

Spudich³

2004

Proc. Natl. Acad. Sci. U.S.A.

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Dictyostelium mitotic kinesin Kif12 is required for cytokinesis. Myosin II localization to the cleavage furrow is severely depressed in Kif12-null (⌬kif12) cells, which accounts in part for the cytokinesis failure. Myosin II-null cells, however, undergo mitosis-coupled cytokinesis when adhering to a surface, whereas the ⌬kif12 cells cannot. During mitosis, the rate of change of internuclear separation in ⌬kif12 cells is reduced compared with wild-type cells, indicating multiple roles of this molecular motor during mitosis and cytokinesis. GFP-Kif12, which rescues wild-type behavior when expressed in the ⌬kif12 strain, is concentrated in the nucleus in interphase cells, translocates to the cytoplasm at the onset of mitosis, appears in the centrosomes and spindle, and later is concentrated in the spindle midbody. Given these results, we hypothesize a mechanism for myosin II translocation to the furrow to set up the contractile ring.Kif12 ͉ cell-cycle regulation ͉ mitosis C ytokinesis and karyokinesis are fundamental to cell division and propagation. Karyokinesis involves nuclear segregation and requires the formation of a microtubule network on which the chromosomes are segregated with the help of kinesin-based motors. Cytokinesis involves division of cellular components of a parental cell into two daughter cells, and it is precisely timed along with nuclear division in almost all cells. Cytokinesis is generally achieved by an actin-myosin-based contractile ring that is assembled along the plane perpendicular to the axis of the spindle poles. Karyokinesis and cytokinesis are tightly synchronized to ensure high fidelity of genomic information transfer.Classic experiments carried out on sand dollar eggs established the importance of the mitotic spindles and astral microtubules in setting up the contractile ring (1, 2). The central spindle has been shown to be important for the completion of cytokinesis in several organisms, including Dictyostelium (3). Although a number of proteins have been shown to be associated with the mitotic spindle and implicated in cytokinesis (4-6), the molecular clues for the crosstalk between the spindle and cortical midzone during mitosis remain elusive.Members of the mitotic kinesin family have been shown to play key roles in the assembly and function of the mitotic spindle. In mammalian cells, MKLP1 is required for the formation of the midbody matrix and the completion of cytokinesis (7,8). Similar gene disruption experiments of MKLP1 orthologs in zebrafish (9), Drosophila (10), and Caenorhabditis elegans (11) also result in a cytokinesis failure. In most cases, furrow ingression is initiated, but cytokinesis fails to complete. Thus, MKLP1 is a key player in passing information from the mitotic spindle to the cleavage furrow.Myosin II is a major component of the cellular machinery responsible for cytokinesis (12, 13). However, little is known about how myosin is translocated to the cleavage furrow during mitosis. Using Dictyostelium as a model system, our laboratory has been studying m...

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Section: Discussionmentioning

confidence: 99%

A mitotic kinesin-like protein required for normal karyokinesis, myosin localization to the furrow, and cytokinesis in Dictyostelium

Lakshmikanth

Warrick²,

Spudich³

2004

Proc. Natl. Acad. Sci. U.S.A.

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“…Recent studies have directly implicated Cdc42 and actin in membrane trafficking through the Golgi. For example, actin has been observed on Golgi-derived membrane vesicles and can assemble on Golgi membranes in vitro (Musch et al, 1997;Godi et al, 1998;Heimann et al, 1999;Fucini et al, 2000;Valderrama et al, 2000). Cdc42 also seems to associate with Golgi-membranes and to induce actin polymerization through the engagement of N-WASP (Fucini et al, 2002;McCallum et al, 1998;Moreau et al, 2000;Wu et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Kanzaki

Watson

Hou

et al. 2002

MBoC

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TC10 is a member of the Rho family of small GTP-binding proteins that has previously been implicated in the regulation of insulin-stimulated GLUT4 translocation in adipocytes. In a manner similar to Cdc42-stimulated actin-based motility, we have observed that constitutively active TC10 (TC10/Q75L) can induce actin comet tails in Xenopus oocyte extracts in vitro and extensive actin polymerization in the perinuclear region when expressed in 3T3L1 adipocytes. In contrast, expression of TC10/Q75L completely disrupted adipocyte cortical actin, which was specific for TC10, because expression of constitutively active Cdc42 was without effect. The effect of TC10/ Q75L to disrupt cortical actin was abrogated after deletion of the amino terminal extension (⌬N-TC10/Q75L), whereas this deletion retained the ability to induce perinuclear actin polymerization. In addition, alteration of perinuclear actin by expression of TC10/Q75L, a dominantinterfering TC10/T31N mutant or a mutant N-WASP protein (N-WASP/⌬VCA) reduced the rate of VSV G protein trafficking to the plasma membrane. Furthermore, TC10 directly bound to Golgi COPI coat proteins through a dilysine motif in the carboxyl terminal domain consistent with a role for TC10 regulating actin polymerization on membrane transport vesicles. Together, these data demonstrate that TC10 can differentially regulate two types of filamentous actin in adipocytes dependent on distinct functional domains and its subcellular compartmentalization. INTRODUCTIONTC10 is a member of the Rho family of GTP-binding proteins and is closely related to Cdc42 (Neudauer et al., 1998). Although TC10 is primarily expressed in adipose and muscle tissue (Neudauer et al., 1998;Imagawa et al., 1999), its function has only been peripherally examined. In vitro binding assays have indicated that active GTP-bound TC10 can bind a number of potential effectors, including mixed lineage kinase 2, myotonic dystrophy-related Cdc42 kinase, p21-activated protein kinases, the Borg family of interacting proteins, the mammalian partition-defective homolog Par6, and the N-WASP isoform of the Wiskott-Aldrich Syndrome Protein (Neudauer et al., 1998;Joberty et al., 1999Joberty et al., , 2000.However, whether TC10 can interact with any of these potential effectors under physiological conditions has yet to be established. Nevertheless, similar to other members of the Rho family, expression of a constitutively active TC10 mutant (TC10/Q75L) in fibroblasts decreased actin stress fibers concomitant with the formation of plasma membrane microspikes (Murphy et al., 1999). However, expression of wildtype TC10 (TC10/WT) was without any effect on fibroblast cell morphology or actin structures. In contrast, expression of wild-type Cdc42 (Cdc42/WT) or a constitutively active Cdc42 mutant (Cdc42/Q61L) in fibroblasts decreased actin stress fibers in parallel with the induction of actin protrusions and lamellipodia (Coghlan et al., 2000). These data indicate that although fibroblasts express the necessary downstream effectors to modulate ac...

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“…In the secretory pathway, actin filaments are required to maintain the organization of the Golgi complex (Valderrama et al, 1998;di Campli et al, 1999) and for protein transport from the Golgi to the plasma membrane and the ER Valderrama et al, 2001). In addition, actin-binding protein spectrin/ankyrin isoforms and several myosins have been localized to the Golgi complex and implicated in transport functions (Beck et al, 1994;Mü sch et al, 1997;Buss et al, 1998;Godi et al, 1998;Stow et al, 1998;Heimann et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Regulation of Protein Transport from the Golgi Complex to the Endoplasmic Reticulum by CDC42 and N-WASP

Luna

Matas

Martı́nez-Menárguez

et al. 2002

MBoC

143

136

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Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mammalian cells. Little, however, is known about the regulation of the Golgi-associated actin cytoskeleton. We provide evidence that Cdc42, a small GTPase that regulates actin dynamics, controls Golgi-to-ER protein transport. We located GFP-Cdc42 in the lateral portions of Golgi cisternae and in COPI-coated and noncoated Golgi-associated transport intermediates. Overexpression of Cdc42 and its activated form Cdc42V12 inhibited the retrograde transport of Shiga toxin from the Golgi complex to the ER, the redistribution of the KDEL receptor, and the ER accumulation of Golgi-resident proteins induced by the active GTP-bound mutant of Sar1 (Sar1[H79G]). Coexpression of wild-type or activated Cdc42 and N-WASP also inhibited Golgi-to-ER transport, but this was not the case in cells expressing Cdc42V12 and N-WASP(ΔWA), a mutant form of N-WASP that lacks Arp2/3 binding. Furthermore, Cdc42V12 recruited GFP-N-WASP to the Golgi complex. We therefore conclude that Cdc42 regulates Golgi-to-ER protein transport in an N-WASP–dependent manner

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Myosin II Is Involved in the Production of Constitutive Transport Vesicles from the TGN

Cited by 171 publications

References 78 publications

A mitotic kinesin-like protein required for normal karyokinesis, myosin localization to the furrow, and cytokinesis in Dictyostelium

A mitotic kinesin-like protein required for normal karyokinesis, myosin localization to the furrow, and cytokinesis in Dictyostelium

Small GTP-binding Protein TC10 Differentially Regulates Two Distinct Populations of Filamentous Actin in 3T3L1 Adipocytes

Regulation of Protein Transport from the Golgi Complex to the Endoplasmic Reticulum by CDC42 and N-WASP

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