Role(s) of Cdc48/p97 in mitosis

Meyer, Hemmo; Popp, Oliver

doi:10.1042/bst0360126

Cited by 31 publications

(23 citation statements)

References 36 publications

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“…As a common activity applied in different pathways, the Cdc48/p97-Ufd1-Npl4 complex is thought to bind and extract ubiquitylated client proteins from cellular structures and to release them for either degradation or recycling (Jentsch and Rumpf, 2007;Ye, 2006). In mitosis, Cdc48/p97-Ufd1-Npl4 has been associated with different functions, such as chromosome segregation, spindle dynamics and organelle reformation, in different organisms and developmental stages (Meyer and Popp, 2008). In Xenopus laevis egg extracts, Cdc48/p97-Ufd1-Npl4 removes Aurora B from chromatin during exit from mitosis in a process that involves modification of Aurora B with ubiquitin chains (Ramadan et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Cdc48/p97–Ufd1–Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells

Dobrynin

Popp

Romer

et al. 2011

Journal of Cell Science

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SummaryDuring exit from mitosis in Xenopus laevis egg extracts, the AAA+ ATPase Cdc48/p97 (also known as VCP in vertebrates) and its adapter Ufd1-Npl4 remove the kinase Aurora B from chromatin to allow nucleus formation. Here, we show that in HeLa cells Ufd1-Npl4 already antagonizes Aurora B on chromosomes during earlier mitotic stages and that this is crucial for proper chromosome segregation. Depletion of Ufd1-Npl4 by small interfering RNA (siRNA) caused chromosome alignment and anaphase defects resulting in missegregated chromosomes and multi-lobed nuclei. Ufd1-Npl4 depletion also led to increased levels of Aurora B on prometaphase and metaphase chromosomes. This increase was associated with higher Aurora B activity, as evidenced by the partial resistance of CENP-A phosphorylation to the Aurora B inhibitor hesperadin. Furthermore, low concentrations of hesperadin partially rescued chromosome alignment in Ufd1-depleted cells, whereas, conversely, Ufd1-depletion partially restored congression in the presence of hesperadin. These data establish Cdc48/p97-Ufd1-Npl4 as a crucial negative regulator of Aurora B early in mitosis of human somatic cells and suggest that the activity of Aurora B on chromosomes needs to be restrained to ensure faithful chromosome segregation.

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Section: Introductionmentioning

confidence: 99%

Cdc48/p97–Ufd1–Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells

Dobrynin

Popp

Romer

et al. 2011

Journal of Cell Science

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“…HVO_1907 is one of four H. volcanii isoforms of a putative AAA ϩ ATPase that show homology to the yeast Ccd48 and E. coli FtsH proteins. In eukaryotes, Cdc48 is a ubiquitin-dependent chaperone that is involved in protein degradation (29), while bacterial FtsH is a Zn 2ϩ metalloprotease that degrades a set of short-lived proteins (24); both are thought to regulate cell division at the level of protein stability. Notably, H. volcanii Cdc48d features a histidinerich C terminus (Fig.…”

Section: Resultsmentioning

confidence: 99%

Improved Strains and Plasmid Vectors for Conditional Overexpression of His-Tagged Proteins in Haloferax volcanii

Allers

Barak

Liddell

et al. 2010

Appl Environ Microbiol

182

216

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Research into archaea will not achieve its full potential until systems are in place to carry out genetics and biochemistry in the same species. Haloferax volcanii is widely regarded as the best-equipped organism for archaeal genetics, but the development of tools for the expression and purification of H. volcanii proteins has been neglected. We have developed a series of plasmid vectors and host strains for conditional overexpression of halophilic proteins in H. volcanii. The plasmids feature the tryptophan-inducible p.tnaA promoter and a 6؋His tag for protein purification by metal affinity chromatography. Purification is facilitated by host strains, where pitA is replaced by the ortholog from Natronomonas pharaonis. The latter lacks the histidine-rich linker region found in H. volcanii PitA and does not copurify with His-tagged recombinant proteins. We also deleted the mrr restriction endonuclease gene, thereby allowing direct transformation without the need to passage DNA through an Escherichia coli dam mutant.

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“…In yeast, Cdc48-Ufd1 mobilizes the transcription factors Spt23 and Mga2 from membranes prior to their moving to the nucleus (33,59,66). Based on these and other observations, Meyer and Popp (46) suggest that the fundamental activity of Cdc48 is the energy-dependent removal of ubiquitylated proteins from membranes. Once removed, these proteins are free to be degraded or deubiquitylated.…”

mentioning

confidence: 99%

“…We also determined whether Cdc48 itself, and/or the Cdc48 accessory factors Shp1 and Ufd1, also were needed. Shp1 and Ufd1 bind directly to Cdc48 (46). Both Shp1 and Ufd1 bind ubiquitin.…”

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Altering Sphingolipid Metabolism in Saccharomyces cerevisiae Cells Lacking the Amphiphysin Ortholog Rvs161 Reinitiates Sugar Transporter Endocytosis

et al. 2009

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Amphiphysins are proteins thought to be involved in synaptic vesicle endocytosis. Amphiphysins share a common BAR domain, which can sense and/or bend membranes, and this function is believed to be essential for endocytosis. Saccharomyces cerevisiae cells lacking the amphiphysin ortholog Rvs161 are inviable when starved for glucose. Altering sphingolipid levels in rvs161 cells remediates this defect, but how lipid changes suppress remains to be elucidated. Here, we show that the sugar starvation-induced death of rvs161 cells extends to other fermentable sugar carbon sources, and the loss of sphingolipid metabolism suppresses these defects. In all cases, rvs161 cells respond to the starvation signal, elicit the appropriate transcriptional response, and properly localize the requisite sugar transporter(s). However, Rvs161 is required for transporter endocytosis. rvs161 cells accumulate transporters at the plasma membrane under conditions normally resulting in their endocytosis and degradation. Transporter endocytosis requires the endocytosis (endo) domain of Rvs161. Altering sphingolipid metabolism by deleting the very-long-chain fatty acid elongase SUR4 reinitiates transporter endocytosis in rvs161 and rvs161 endo ؊ cells. The sphingolipid-dependent reinitiation of endocytosis requires the ubiquitin-regulating factors Doa1, Doa4, and Rsp5. In the case of Doa1, the phospholipase A 2 family ubiquitin binding motif is dispensable. Moreover, the conserved AAA-ATPase Cdc48 and its accessory proteins Shp1 and Ufd1 are required. Finally, rvs161 cells accumulate monoubiquitin, and this defect is remediated by the loss of SUR4. These results show that defects in sphingolipid metabolism result in the reinitiation of ubiquitin-dependent sugar transporter endocytosis and suggest that this event is necessary for suppressing the nutrient starvation-induced death of rvs161 cells.

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Role(s) of Cdc48/p97 in mitosis

Cited by 31 publications

References 36 publications

Cdc48/p97–Ufd1–Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells

Cdc48/p97–Ufd1–Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells

Improved Strains and Plasmid Vectors for Conditional Overexpression of His-Tagged Proteins in Haloferax volcanii

Altering Sphingolipid Metabolism in Saccharomyces cerevisiae Cells Lacking the Amphiphysin Ortholog Rvs161 Reinitiates Sugar Transporter Endocytosis

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