The aberrant expression and localization of prohibitin during apoptosis of human cholangiocarcinoma Mz‐ChA‐1 cells

Song, Wei; Tian, Ling; Li, Shanshan; Shen, Dong‐Yan; Chen, Qing‐Xi

doi:10.1016/j.febslet.2013.12.021

Cited by 12 publications

(13 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The subcellular localization of PHB is affected by apoptotic signals, and inhibition of this translocation affects apoptosis. During the apoptosis of cancer cells induced by abrin or ESC-3, PHB1 translocates from the cytoplasm or mitochondria to the nucleus (Song et al, 2014). During the apoptosis of cancer cells induced by estradiol or capsaicin, PHB2 translocates from the cytoplasm or mitochondria to the nucleus (Kim et al, 2009;Kuramori et al, 2009).…”

Section: Phb3 Maintains Stem Cell Niche Activity Via Regulating Genommentioning

confidence: 99%

Nuclear Prohibitin3 Maintains Genome Integrity and Cell Proliferation in the Root Meristem through Minichromosome Maintenance 2

et al. 2019

View full text Add to dashboard Cite

The nucleo-mitochondrial dual-localized proteins can act as gene expression regulators; however, few instances of these proteins have been described in plants. Arabidopsis (Arabidopsis thaliana) PROHIBITIN 3 (PHB3) is involved in stress responses and developmental processes, but it is unknown how these roles are achieved at the molecular level in the nucleus. In this study, we show that nucleo-mitochondrial PHB3 plays an essential role in regulating genome stability and cell proliferation. PHB3 is upregulated by DNA damage agents, and the stress-induced PHB3 proteins accumulate in the nucleus. Loss of function of PHB3 results in DNA damage and defective maintenance of the root stem cell niche. Subsequently, the expression patterns and levels of the root stem cell regulators are altered and down-regulated, respectively. In addition, the phb3 mutant shows aberrant cell division and altered expression of cell cycle-related genes, such as CycB1 and Cyclin dependent kinase 1. Moreover, the minichromosome maintenance (MCM) genes, e.g. MCM2, MCM3, MCM4, MCM5, MCM6, and MCM7, are up-regulated in the phb3 mutant. Reducing the MCM2 expression level substantially recovers the DNA damage in the phb3 mutant and partially rescues the altered cell proliferation and root deficiency of phb3 seedlings. PHB3 acts as a transcriptional coregulator that represses MCM2 expression by competitively binding to the promoter E2F-cis-acting elements with E2Fa so as to modulate primary root growth. Collectively, these findings indicate that nuclear-localized PHB3 acts as a transcriptional coregulator that suppresses MCM2 expression to sustain genome integrity and cell proliferation for stem cell niche maintenance in Arabidopsis.

show abstract

Section: Phb3 Maintains Stem Cell Niche Activity Via Regulating Genommentioning

confidence: 99%

Nuclear Prohibitin3 Maintains Genome Integrity and Cell Proliferation in the Root Meristem through Minichromosome Maintenance 2

et al. 2019

View full text Add to dashboard Cite

show abstract

“…This transcriptional regulation function of PHB1 in the nucleus may provide a link between the proliferative and apoptotic pathways [ 25 , 40 , 41 ]. In general, PHB1 co-localized with p53, Rb, E2F, AIF, c-myc, and c-fos in the nucleus [ 25 , 27 , 42 – 45 ]. These tumor-suppressor and oncogene proteins are of great importance for mammalian cell apoptosis and survival, and they usually function in a coordinated manner [ 46 ].…”

Section: Phb and Its Transcriptional Regulation In The Nucleusmentioning

confidence: 99%

“…During apoptosis induced by ESC-3, an active ingredient of crocodile bile, in human cholangiocarcinoma Mz-ChA-1 cells, PHB1 is dramatically downregulated, and the region of co-localization between PHB1 and AIF, p53, Rb, and c-fos shifted from the cytoplasm to the nucleus. In this case, PHB1 was expressed primarily in the cytoplasm and only slightly in the nucleus of Mz-ChA-1 cells [ 45 ]. In human breast cancer cells, the absence of brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) promoted the translocation of PHB2 to the nucleus after estradiol stimulation and resulted in the suppression of cancer cell growth.…”

Section: Phb and Nuclear Trafficking And Apoptosismentioning

confidence: 99%

Multifaceted role of prohibitin in cell survival and apoptosis

et al. 2015

View full text Add to dashboard Cite

Human eukaryotic prohibitin (prohibitin-1 and prohibitin-2) is a membrane protein with different cellular localizations. It is involved in multiple cellular functions, including energy metabolism, proliferation, apoptosis, and senescence. The subcellular localization of prohibitin may determine its functions. Membrane prohibitin regulate the cellular signaling of membrane transport, nuclear prohibitin control transcription activation and the cell cycle, and mitochondrial prohibitin complex stabilize the mitochondrial genome and modulate mitochondrial dynamics, mitochondrial morphology, mitochondrial biogenesis, and the mitochondrial intrinsic apoptotic pathway. Moreover, prohibitin can translocates into the nucleus or the mitochondria under apoptotic signals and the subcellular shuttling of prohibitin is necessary for apoptosis process. Apoptosis is the process of programmed cell death that is important for the maintenance of normal physiological functions. Consequently, any alteration in the content, post-transcriptional modification (i.e. phosphorylation) or the nuclear or mitochondrial translocation of prohibitin may influence cell fate. Understanding the mechanisms of the expression and regulation of prohibitin may be useful for future research. This review provides an overview of the multifaceted and essential roles played by prohibitin in the regulation of cell survival and apoptosis.

show abstract

“…Prohibitin, which increased 2.1-fold at 0 h before returning to control levels at 3 h, is found in a number of cellular compartments and has been ascribed diverse roles, including as a mitochondrial chaperone (Nijtmans et al, 2000) and in regulation of transcription and cell cycle progression (Artal-Sanz and Tavernarakis, 2009). Most importantly, decreased prohibitin protein levels appear to induce apoptosis (Sánchez-Quiles et al, 2010), perhaps through greater sensitivity to oxidative damage (Theiss et al, 2006), and the 3′-untranslated region of prohibitin mRNA has been identified as a tumor suppressor with anti-proliferative activity (Song et al, 2014). Based on these findings, we suggest that the rapid increase in prohibitin abundance in G. demissa during heat stress may be a protective response to delay or avoid heat-induced apoptosis.…”

Section: Discussionmentioning

confidence: 50%

Rapid proteomic responses to a near-lethal heat stress in the salt marsh musselGeukensia demissa

Fields

Burmester

Cox

et al. 2016

Journal of Experimental Biology

View full text Add to dashboard Cite

Acute heat stress perturbs cellular function on a variety of levels, leading to protein dysfunction and aggregation, oxidative stress and loss of metabolic homeostasis. If these challenges are not overcome quickly, the stressed organism can die. To better understand the earliest tissue-level responses to heat stress, we examined the proteomic response of gill from Geukensia demissa, an extremely eurythermal mussel from the temperate intertidal zone of eastern North America. We exposed 15°C-acclimated individuals to an acute near-lethal heat stress (45°C) for 1 h, and collected gill samples from 0 to 24 h of recovery. The changes in protein expression we found reveal a coordinated physiological response to acute heat stress: proteins associated with apoptotic processes were increased in abundance during the stress itself (i.e. at 0 h of recovery), while protein chaperones and foldases increased in abundance soon after (3 h). The greatest number of proteins changed abundance at 6 h; these included oxidative stress proteins and enzymes of energy metabolism. Proteins associated with the cytoskeleton and extracellular matrix also changed in abundance starting at 6 h, providing evidence of cell proliferation, migration and tissue remodeling. By 12 h, the response to acute heat stress was diminishing, with fewer stress and structural proteins changing in abundance. Finally, the proteins with altered abundances identified at 24 h suggest a return to the pre-stress anabolic state.

show abstract

The aberrant expression and localization of prohibitin during apoptosis of human cholangiocarcinoma Mz‐ChA‐1 cells

Cited by 12 publications

References 25 publications

Nuclear Prohibitin3 Maintains Genome Integrity and Cell Proliferation in the Root Meristem through Minichromosome Maintenance 2

Nuclear Prohibitin3 Maintains Genome Integrity and Cell Proliferation in the Root Meristem through Minichromosome Maintenance 2

Multifaceted role of prohibitin in cell survival and apoptosis

Rapid proteomic responses to a near-lethal heat stress in the salt marsh musselGeukensia demissa

Contact Info

Product

Resources

About