Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis

Neef, Riidiger; Preisinger, Christian; Sutcliffe, Josephine E.; Kopajtich, Robert; Nigg, Erich A.; Mayer, Thomas; Barr, Francis A.

doi:10.1083/jcb.200306009

Cited by 293 publications

(363 citation statements)

References 67 publications

(94 reference statements)

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“…Another important protein of this complex is PLK1 (polo-like kinase 1) which binds to microtubules and interacts with MKLP2. Phosphorylation of MKLP2 by PLK1 is required for the localization of PLK1 to the central spindle during anaphase and telophase and the complex of these two proteins is necessary for the completion of cytokinesis [26]. It is also shown that PLK1 is important for the binding of ECT2 to CYK-4 and its recruitment to the midzone, thus promoting the initiation and completion of cytokinesis.…”

Section: Early Cytokinesismentioning

confidence: 99%

“…Microtubule-associated proteins PRC1 [13,14] Centralspindlin complex CYK-4 [2,15] MKLP1 [2,15] Chromosome passenger complex INCENP [16,17] Survinin [16,17] Borealin [16,17] Aurora B [16,17] ESRCTs and associated proteins CEP55 [30][31][32] TSG101 [31,32] ALIX [31,32] CHMP1B [33] Spastin [33] CHMP4B [31,32,34] FYVE-CENT [34] TTC19 [34] Kinesins KIF4A [14] MKLP2 [17] MPP1 [22] KIF14 [23] KIF13A [34] Additional proteins NuSAP [18] Orbit [19] ASP [20] TBCD [21] ECT2 [24] FIP3 [25] PLK1 [26,27] Septins [28] Anillin [29] during anaphase and cytokinesis and is important for the last step of abscission. CEP55 binds directly MKLP1 and is controlled by centralspindlin, since knockdown of centralspindlin abolishes CEP55 from the midbody [30].…”

Section: The Abscission Step Of Cytokinesismentioning

confidence: 99%

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Cytokinesis and cancer

Sagona

Stenmark

2010

FEBS Letters

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a b s t r a c tCytokinesis is the final stage of cell division during which the two daughter cells separate completely. Although less well understood than some of the earlier phases of the cell cycle, recent discoveries have shed light on the mechanisms that orchestrate this process, including cleavage furrow formation, midbody maturation and abscission. One of the reasons why research on cytokinesis has been attracting increasing attention is the concept that failure of this process in mammals is associated with carcinogenesis. In this minireview, we will discuss the possible links between cytokinesis and cancer, and highlight key mechanisms that connect these processes.

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Section: Early Cytokinesismentioning

confidence: 99%

Section: The Abscission Step Of Cytokinesismentioning

confidence: 99%

Cytokinesis and cancer

Sagona

Stenmark

2010

FEBS Letters

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“…This could be attributed to the presence of additional motor proteins with similar function to CHO1 at the spindle midzone. It has recently been reported that Rab6-KIFL (MKLP2: Hill et al, 2000;Neef et al, 2003) and PMM1 (Abaza et al, 2003) at the central spindle contain the microtubule bundling activity and are required for cytokinesis. Simultaneous elimination of all three motors may result in complete disorganization of central spindles and inhibition of cleavage furrow formation.…”

Section: Role Of Cho1 In Cytokinesismentioning

confidence: 99%

“…Isolated midbodies contain at least 158 different molecules (Skop et al, 2002); some of those might be responsible for maintaining the structural integrity of the midbody by connecting molecules in the midbody. Possible candidates might be PRC1, Rab6-KIFL, or MPP1, which were shown to bundle midzone microtubules (Jiang et al, 1998;Mollinari et al, 2002;Abaza et al, 2003;Neef et al, 2003). One possible scenario is that the T3 sequence of CHO1 is directly involved in association of CHO1 with those midbody components.…”

Section: Role Of the Nls-containing Regionmentioning

confidence: 99%

Role of the Midbody Matrix in Cytokinesis: RNAi and Genetic Rescue Analysis of the Mammalian Motor Protein CHO1

Matulienė

Kuriyama

2004

MBoC

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CHO1 is a kinesin-like motor protein essential for cytokinesis in mammalian cells. To analyze how CHO1 functions, we established RNAi and genetic rescue assays. CHO1-depleted cells reached a late stage of cytokinesis but fused back to form binucleate cells because of the absence of the midbody matrix in the middle of the intercellular bridge. Expression of exogenous CHO1 restored the formation of the midbody matrix and rescued cytokinesis in siRNA-treated cells. By analyzing phenotypes rescued with different constructs, it was shown that both motor and stalk domains function in midbody formation, whereas the tail is essential for completion of cytokinesis after the midbody matrix has formed. During the terminal stage of cytokinesis, different subregions of the tail play distinctive roles in stabilizing the midbody matrix and maintaining an association between the midbody and cell cortex. These results demonstrate that CHO1 consists of functionally differentiated subregions that act in concert to ensure complete cell separation.

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“…The role of rabkinesin6 as a rab6A-specific effector during interphase was recently challenged by the finding that rabkinesin6 does not colocalize with rab6 and is only present in minute amounts in interphase cells. In contrast, rabkinesin6 is greatly up-regulated during mitosis where it plays a role in cytokinesis (Hill et al, 2000;Fontijn et al, 2001;Neef et al, 2003). Nevertheless, the specific binding of rabkinesin6 to rab6A but not A' is consistent with the ability of rab6A but not A' to induce Golgi-to-ER recycling when overexpressed as a GTP-restricted mutant (Echard et al, 2000).…”

mentioning

confidence: 97%

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

Young

Stauber

Nery

et al. 2005

MBoC

105

126

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The small GTPase rab6A but not the isoform rab6A has previously been identified as a regulator of the COPIindependent recycling route that carries Golgi-resident proteins and certain toxins from the Golgi to the endoplasmic reticulum (ER). The isoform rab6A has been implicated in Golgi-to-endosomal recycling. Because rab6A but not A , binds rabkinesin6, this motor protein is proposed to mediate COPI-independent recycling. We show here that both rab6A and rab6A GTP-restricted mutants promote, with similar efficiency, a microtubule-dependent recycling of Golgi resident glycosylation enzymes upon overexpression. Moreover, we used small interfering RNA mediated down-regulation of rab6A and A' expression and found that reduced levels of rab6 perturbs organization of the Golgi apparatus and delays Golgi-to-ER recycling. Rab6-directed Golgi-to-ER recycling seems to require functional dynactin, as overexpression of p50/dynamitin, or a C-terminal fragment of Bicaudal-D, both known to interact with dynactin inhibit recycling. We further present evidence that rab6-mediated recycling seems to be initiated from the trans-Golgi network. Together, this suggests that a recycling pathway operates at the level of the trans-Golgi linking directly to the ER. This pathway would be the preferred route for both toxins and resident Golgi proteins. INTRODUCTIONAnterograde flow of material through the exocytic pathway is offset by the constant recycling of both proteins and lipids. This recycling helps to ensure that steady-state distributions of resident proteins are maintained within the pathway at the same time as keeping a lipid balance. Besides intra-Golgi recycling between cisternae (Hoe et al., 1995;Love et al., 1998;Lanoix et al., 1999;Lin et al., 1999), Golgi glycosylation enzymes also can recycle directly to the endoplasmic reticulum (ER). It is estimated that at least 5% of Golgi resident enzymes reside in the ER, at steady state (Pelletier et al., 2000). This pool constitutes recycled material originating from the Golgi apparatus (Cole et al., 1998;Storrie et al., 1998).The extent of ER recycling of Golgi resident membrane proteins is sufficient to allow for complete assembly of functional Golgi stacks. Thus, upon addition of nocodazole to depolymerize microtubules, the central and juxtanuclear Golgi apparatus relocates to the 100 or so peripheral ER exit sites scattered throughout the cell. This microtubule-independent relocation occurs in the absence of any detectable elements tracking outwards from the central Golgi apparatus. Rather, the Golgi apparatus undergoes a molecular deconstruction in the trans-to-cis-direction, i.e., resident glycosylation enzymes of the trans-cisternae/trans-Golgi network (TGN) relocate with faster kinetics than do enzymes of the medial-cisternae (Yang and Storrie, 1998). Enzymes seemingly enter the ER close to the microtubule organizing center (MTOC), diffuse through the ER, and then reemerge at peripheral ER exit sites. Here, Golgi stacks are then reassembled into discrete, yet fully functiona...

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Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis

Cited by 293 publications

References 67 publications

Cytokinesis and cancer

Cytokinesis and cancer

Role of the Midbody Matrix in Cytokinesis: RNAi and Genetic Rescue Analysis of the Mammalian Motor Protein CHO1

Regulation of Microtubule-dependent Recycling at theTrans-Golgi Network by Rab6A and Rab6A'

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