Identification and phylogenetic analysis of Dictyostelium discoideum kinesin proteins

Kollmar, Martin; Glöckner, Gernot

doi:10.1186/1471-2164-4-47

Cited by 32 publications

(17 citation statements)

References 80 publications

(94 reference statements)

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“…2b). Previous analyses highlighted a short 23-residue hydrophobic region located 18 residues from the Kif9 carboxyl terminus (aa1182–1204) that could serve as a transmembrane domain [17]. To test whether this region anchors the Kif9 protein, we expressed a truncated version of Kif9 construct lacking the final 43 resides (Kif9 1179 ).…”

Section: Resultsmentioning

confidence: 99%

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A kinesin-mediated mechanism that couples centrosomes to nuclei

Tikhonenko

Magidson

Gräf

et al. 2012

Cell. Mol. Life Sci.

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The M-type kinesin isoform, Kif9, has recently been implicated in maintaining a physical connection between the centrosome and nucleus in Dictyostelium discoideum. However, the mechanism by which Kif9 functions to link these two organelles remains obscure. Here we demonstrate that the Kif9 protein is localized to the nuclear envelope and is concentrated in the region underlying the centrosome point of attachment. Nuclear anchorage appears mediated through a specialized trans-membrane domain located in the carboxyl terminus. Kif9 interacts with microtubules in in vitro binding assays and effects an endwise depolymerization of the polymer. These results suggest a model whereby Kif9 is anchored to the nucleus and generates a pulling force that reels the centrosome up against the nucleus. This is a novel activity for a kinesin motor, one important for progression of cells into mitosis and to ensure centrosome-nuclear parity in a multinuclear environment.

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Section: Resultsmentioning

confidence: 99%

“…8). We postulate that Kif9 is anchored into the NE through the hydrophobic motif located near the protein’s carboxyl-terminus [10, 17]. The extreme C-terminal tail would then be positioned in the perinuclear space and available to interact with Sun1 to strengthen and support this anchorage.…”

Section: Discussionmentioning

confidence: 99%

A kinesin-mediated mechanism that couples centrosomes to nuclei

Tikhonenko

Magidson

Gräf

et al. 2012

Cell. Mol. Life Sci.

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“…The full-length kif12 was cloned further into a pTXbased vector (14). While this work was being completed, this gene and five other mitotic kinesins were reported in the Dictyostelium genome (15).…”

Section: Methodsmentioning

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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“…The top row represents the full-length, 1238aa construct. A detailed representation of the domain organization of DdKif10 can be found in reference [17]. Despite multiple attempts, we were only able to detect the expression of the middle-length construct in D. discoideum cells.…”

Section: Resultsmentioning

confidence: 99%

“…DdKif10 is a 1238aa (139 kDa) polypeptide with an amino-terminal motor domain, a central region with two prominent predicted coiled-coil motifs, and a carboxy terminal tail that likely contains cargo-binding regions [17,18]. The motor/neck domain clearly groups to the Kinesin-8 family, with 45% identity over the first 425 residues to the human Kif18A protein.…”

Section: Resultsmentioning

confidence: 99%

Bioenergetics of the Dictyostelium Kinesin-8 Motor Isoform

Koonce

Tikhonenko

2020

Biomolecules

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The functional organization of microtubules in eukaryotic cells requires a combination of their inherent dynamic properties, interactions with motor machineries, and interactions with accessory proteins to affect growth, shrinkage, stability, and architecture. In most organisms, the Kinesin-8 family of motors play an integral role in these organizations, well known for their mitotic activities in microtubule (MT) length control and kinetochore interactions. In Dictyostelium discoideum, the function of Kinesin-8 remains elusive. We present here some biochemical properties and localization data that indicate that this motor (DdKif10) shares some motility properties with other Kinesin-8s but also illustrates differences in microtubule localization and depolymerase action that highlight functional diversity.

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Identification and phylogenetic analysis of Dictyostelium discoideum kinesin proteins

Cited by 32 publications

References 80 publications

A kinesin-mediated mechanism that couples centrosomes to nuclei

A kinesin-mediated mechanism that couples centrosomes to nuclei

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

Bioenergetics of the Dictyostelium Kinesin-8 Motor Isoform

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