PLK-1 Regulation of Asymmetric Cell Division in the Early C. elegans Embryo

Kim, Amelia J.; Griffin, Erik E.

doi:10.3389/fcell.2020.632253

Cited by 10 publications

(5 citation statements)

References 89 publications

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“…PLK-1 targets the cytoplasmic filaments, the inner ring complex and the central channel nucleoporins To identify the nuclear pore subcomplexes targeted by PLK-1, we used spinning disk confocal microscopy to monitor the dynamics of fluorescently tagged nucleoporins from each NPC subcomplex during mitosis in control embryos, or upon plk-1 inactivation. Since PLK-1 regulates several processes in the early embryo (7,15,(37)(38)(39)(40)(41)(42)(43), we used partial RNAi to exclude indirect effects, reasoning that direct PLK-1 targets should be the most sensitive to mild plk-1 inactivation.…”

Section: Plk-1 Triggers the Disassembly Of Soluble Nucleoporins Indep...mentioning

confidence: 99%

Mechanisms of Nuclear Pore Complex disassembly by the mitotic Polo-Like Kinase 1 (PLK-1) inC. elegansembryos

Nkoula

Velez-Aguilera

Ossareh-Nazari

et al. 2023

Preprint

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The nuclear envelope, which protects and organizes the interphase genome, is dismantled during mitosis. In the C. elegans zygote, nuclear envelope breakdown (NEBD) of the parental pronuclei is spatially and temporally regulated during mitosis to promote the unification of the parental genomes. During NEBD, Nuclear Pore Complex (NPC) disassembly is critical for rupturing the nuclear permeability barrier and removing the NPCs from the membranes near the centrosomes and between the juxtaposed pronuclei. By combining live imaging, biochemistry, and phosphoproteomics, we characterized NPC disassembly and unveiled the exact role of the mitotic kinase PLK-1 in this process. We show that PLK-1 disassembles the NPC by targeting multiple NPC sub-complexes, including the cytoplasmic filaments, the central channel, and the inner ring. Notably, PLK-1 is recruited to and phosphorylates intrinsically disordered regions of several multivalent linker nucleoporins, a mechanism that appears to be an evolutionarily conserved driver of NPC disassembly during mitosis.

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Section: Plk-1 Triggers the Disassembly Of Soluble Nucleoporins Indep...mentioning

confidence: 99%

Mechanisms of Nuclear Pore Complex disassembly by the mitotic Polo-Like Kinase 1 (PLK-1) inC. elegansembryos

Nkoula

Velez-Aguilera

Ossareh-Nazari

et al. 2023

Preprint

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“…PLK-1 becomes enriched in the anterior cytoplasm of one-cell embryos and, at the two-cell stage, is enriched in the anterior cell (called AB) relative to the posterior cell (called P1) ( Movie S1 A ) ( 42 – 47 ). PLK-1 anterior accumulation depends on MEX-5 ( 42 ).…”

Section: Resultsmentioning

confidence: 99%

Modeling protein dynamics in Caenorhabditis elegans embryos reveals that the PLK-1 gradient relies on weakly coupled reaction–diffusion mechanisms

Barbieri

Ravi

Griffin

et al. 2022

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

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Significance Intracellular gradients have essential roles in cell and developmental biology, but their formation is not fully understood. We have developed a computational approach facilitating interpretation of protein dynamics and gradient formation. We have combined this computational approach with experiments to understand how Polo-Like Kinase 1 (PLK-1) forms a cytoplasmic gradient in Caenorhabditis elegans embryos. Although the PLK-1 gradient depends on the Muscle EXcess-5/6 (MEX-5/6) proteins, we reveal differences in PLK-1 and MEX-5 gradient formation that can be explained by a model with two components, PLK-1 bound to MEX-5 and unbound PLK-1. Our combined approach suggests that a weak coupling between PLK-1 and MEX-5 reaction–diffusion mechanisms dictates the dynamic exchange of PLK-1 with the cytoplasm, explaining PLK-1 high diffusivity and smooth gradient.

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“…MEX-5 and MEX-6 are highly similar zinc finger proteins that bind RNA, and they are required for generating the asymmet ry of cell fate determinants downstream of PAR-1 (Schubert et al, 2000). PLK-1 is a mitotic kinase enriched in the anterior by MEX-5/6, and PLK-1 is also required for regulating the asymmetry of several cytoplasmic factors (Kim & Griffin, 2020). In wild-type one-cell embryos, PAR-1 has a posterior cytoplasmic gradient, while MEX-5/6 and PLK-1 localize in anterior cytoplasmic gradients; the AB cell inherits more MEX-5/6 and PLK-1 than the P1 cell (Cuenca et al, 2003; Guo & Kemphues, 1995; Nishi et al, 2008; Schubert et al, 2000) We verified that in our par-1 (RNAi) embryos, MEX-5 and PLK-1 were uniform in the one-cell embryo and that the AB and P1 cells received equal amounts (Fig.…”

Section: Resultsmentioning

confidence: 99%

Multiple pathways for reestablishing PAR polarity inC. elegansembryo

Koch¹,

Rose²

2022

Preprint

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Asymmetric cell divisions, where cells divide with respect to a polarized axis and give rise to daughter cells with different fates, are critically important during development. In many such divisions, the conserved PAR polarity proteins accumulate in distinct cortical domains in response to a symmetry breaking cue. The one-cell C. elegans embryo has been a paradigm for understanding mechanisms of PAR polarization, but much less is known about polarity reestablishment during subsequent divisions. Here, we investigate the polarization of the P1 cell of the two-cell embryo. A posterior PAR-2 domain forms in the first four minutes of the birth of P1, and polarization becomes stronger over time. Initial polarization depends on the PKC-3 and PAR-1 kinases. However, in par-1 mutants, delayed polarization can occur, at a time when centrosome-associated AIR-1 is near the posterior cortex and myosin flows towards the anterior. Loss of myosin and par-1 function together results in more severe polarity defects. Based on these and other results, we propose that PAR polarity in the P1 cell is generated by at least two redundant mechanisms: There is a novel early pathway dependent on PAR-1, PKC-3 and cytoplasmic polarity, and a late pathway that resembles symmetry breaking in the one-cell embryo and requires myosin flow and PKC-3.

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PLK-1 Regulation of Asymmetric Cell Division in the Early C. elegans Embryo

Cited by 10 publications

References 89 publications

Mechanisms of Nuclear Pore Complex disassembly by the mitotic Polo-Like Kinase 1 (PLK-1) inC. elegansembryos

Mechanisms of Nuclear Pore Complex disassembly by the mitotic Polo-Like Kinase 1 (PLK-1) inC. elegansembryos

Modeling protein dynamics in Caenorhabditis elegans embryos reveals that the PLK-1 gradient relies on weakly coupled reaction–diffusion mechanisms

Multiple pathways for reestablishing PAR polarity inC. elegansembryo

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