Microtubule-Driven Multimerization Recruits ase1p onto Overlapping Microtubules

Kapitein, Lukas C.; Janson, Marcel E.; Wildenberg, Siet van den; Hoogenraad, Casper C.; Schmidt, Christoph F.; Peterman, Erwin J. G.

doi:10.1016/j.cub.2008.09.046

Cited by 95 publications

(105 citation statements)

References 16 publications

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“…PRC1 is phosphorylated on Thr-470 and Thr-481 by Cdc2 in early mitosis. In fact, our early study showed that phosphorylation of PRC1 at Thr-470 promotes the formation of PRC1 oligomers (15), which may promote the assembly of PRC1 protein onto overlapping microtubules at the central spindle (31). The fact that phosphorylation of Thr-470 and Thr-480 is not involved in PRC1-CLASP1 interaction suggests that central spindle plasticity is orchestrated by several interactive but perhaps parallel pathways.…”

Section: Discussionmentioning

confidence: 99%

PRC1 Cooperates with CLASP1 to Organize Central Spindle Plasticity in Mitosis

Liu

Wang

Jiang

et al. 2009

Journal of Biological Chemistry

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During cell division, chromosome segregation is governed by the interaction of spindle microtubules with the kinetochore. A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis. Central spindle organization requires mitotic kinesins, microtubulebundling protein PRC1, and Aurora B kinase complex. However, the precise role of PRC1 in central spindle organization has remained elusive. Here we show that PRC1 recruits CLASP1 to the central spindle at early anaphase onset. CLASP1 belongs to a conserved microtubule-binding protein family that mediates the stabilization of overlapping microtubules of the central spindle. PRC1 physically interacts with CLASP1 and specifies its localization to the central spindle. Repression of CLASP1 leads to sister-chromatid bridges and depolymerization of spindle midzone microtubules. Disruption of PRC1-CLASP1 interaction by a membrane-permeable peptide abrogates accurate chromosome segregation, resulting in sister chromatid bridges. These findings reveal a key role for the PRC1-CLASP1 interaction in achieving a stable anti-parallel microtubule organization essential for faithful chromosome segregation. We propose that PRC1 forms a link between stabilization of CLASP1 association with central spindle microtubules and anti-parallel microtubule elongation.

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Section: Discussionmentioning

confidence: 99%

PRC1 Cooperates with CLASP1 to Organize Central Spindle Plasticity in Mitosis

Liu

Wang

Jiang

et al. 2009

Journal of Biological Chemistry

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“…The phragmoplast microtubule array Lee and Liu 759 (1) demonstrated that MT-binding stimulates multimerization of Ase1, further recruiting the protein to overlapping MTs [27], a phenomenon that was also observed in vitro for MAP65-3 [6 ]. As a result, the anti-parallel MTs are stabilized after being cross-linked by congregated MAP65-3.…”

Section: Anti-parallel Mts In the Phragmoplastmentioning

confidence: 92%

The rise and fall of the phragmoplast microtubule array

Lee

Liu

2013

Current Opinion in Plant Biology

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The cytokinetic apparatus, the phragmoplast, contains a bipolar microtubule (MT) framework that has the MT plus ends concentrated at or near the division site. This anti-parallel MT array provides tracks for the transport of Golgi-derived vesicles toward the plus ends so that materials enclosed are subsequently deposited at the division site. Here we will discuss a proposed model of the centrifugal expansion of the phragmoplast that takes place concomitantly with the assembly of the cell plate, the ultimate product of vesicle fusion. The expansion is a result of continuous MT assembly at the phragmoplast periphery while the MTs toward the center of the phragmoplast are disassembled. These events are the result of MT-dependent MT polymerization, bundling of antiparallel MTs coming from opposite sides of the division plane that occurs selectively at the phragmoplast periphery, positioning of the plus ends of cross-linked MTs at or near the division site by establishing a minimal MT-overlapping zone, and debundling of anti-parallel MTs that is triggered by phosphorylation of MT-associated proteins. The debundled MTs are disassembled at last by factors including the MT severing enzyme katanin. IntroductionThe innovation of the phragmoplast marks a significant advancement in the evolution from green algae to land plants [1]. The phragmoplast contains a core of two mirrored sets of anti-parallel microtubules (MTs) whose plus ends are concentrated at or near the midzone of this cytokinetic apparatus (Figure 1) [2]. The ultimate mission of this bipolar MT array is to allow Golgi-derived vesicles to be transported unidirectionally toward MT plus ends so that the materials enclosed in these vesicles are deposited for the assembly of the cell plate. Phragmoplast MTs, like those MTs in spindles during mitosis, undergo continuous remodeling throughout cytokinesis [3,4]. Upon the completion of anaphase, MTs are polymerized and coalesced in the spindle midzone, and a bipolar array is established as the Kinesin-5 motor acts on anti-parallel MTs to slide them against each other ( Figure 1a) [5,6 ,7]. Concomitant with the addition of more MTs to the array, the MTs are shortened at their minus ends, which are facing the reforming daughter nuclei (Figure 1b). One of the most spectacular phenomena in cytokinesis is the centrifugal expansion of the phragmoplast MT array from the cell center to the edge. During the expansion, new MT filaments are added to the periphery of the phragmoplast while older ones in the inner part of the phragmoplast array are disassembled ( Figure 1c). This is particularly challenging because those opposing activities occur simultaneously within a few microns of each other. The assembly of new MTs uses tubulin subunits released from the depolymerization of older MTs [3].Before MT-associated proteins (MAPs) and MT-based motors were identified, microscopic observations had revealed many structural details of the phragmoplast in elegant systems like the endosperm of the African blood lily Haemanthus and tobacc...

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“…In vitro experiments at the single molecule level reveal that both PRC1 and Ase1p move diffusively along a single microtubule and have a preference for anti-parallel bundling compared with parallel bundling (Bieling et al, 2010;Kapitein et al, 2008;Subramanian et al, 2010). PRC1 interacts with various motors and MAPs as discussed below.…”

Section: Prc1mentioning

confidence: 98%