A Novel Zinc Finger Protein Is Encoded by the Arabidopsis LSD1 Gene and Functions as a Negative Regulator of Plant Cell Death

Abstract Water deficit is one of the main challenges for apple (Malus × domestica) growth and productivity. Breeding drought-tolerant cultivars depends on a thorough understanding of the drought responses of apple trees. Here, we identified the zinc-finger protein B-BOX 7/CONSTANS-LIKE 9 (MdBBX7/MdCOL9), which plays a positive role in apple drought tolerance. The overexpression of MdBBX7 enhanced drought tolerance, whereas knocking down MdBBX7 expression reduced it. Chromatin immunoprecipitation-sequencing (ChIP-seq) analysis identified one cis-element of MdBBX7, CCTTG, as well as its known binding motif, the T/G box. ChIP-seq and RNA-seq identified 1,197 direct targets of MdBBX7, including ETHYLENE RESPONSE FACTOR (ERF1), EARLY RESPONSIVE TO DEHYDRATION 15 (ERD15), and GOLDEN2-LIKE 1 (GLK1) and these were further verified by ChIP-qPCR and electronic mobility shift assays. Yeast two-hybrid screen identified an interacting protein of MdBBX7, RING-type E3 ligase MYB30-INTERACTING E3 LIGASE 1 (MIEL1). Further examination revealed that MdMIEL1 could mediate the ubiquitination and degradation of MdBBX7 by the 26S proteasome pathway. Genetic interaction analysis suggested that MdMIEL1 acts as an upstream factor of MdBBX7. In addition, MdMIEL1 was a negative regulator of the apple drought stress response. Taken together, our results illustrate the molecular mechanisms by which the MdMIEL1–MdBBX7 module influences the response of apple to drought stress.

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Zinc finger protein RP-8, the Bombyx mori ortholog of programmed cell death 2, regulates cell proliferation

Developmental & Comparative Immunology ◽

10.1016/j.dci.2019.103542 ◽

2020 ◽

Vol 104 ◽

pp. 103542 ◽

Cited By ~ 9

Author(s):

Muhammad Nadeem Abbas ◽

Hanghua Liang ◽

Saima Kausar ◽

Zhen Dong ◽

Hongjuan Cui

Keyword(s):

Cell Proliferation ◽

Cell Death ◽

Programmed Cell Death ◽

Bombyx Mori ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Finger Protein

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The zinc finger protein NRIF interacts with the neurotrophin receptor p75NTR and participates in programmed cell death

The EMBO Journal ◽

10.1093/emboj/18.21.6050 ◽

1999 ◽

Vol 18 (21) ◽

pp. 6050-6061 ◽

Cited By ~ 112

Author(s):

E. Casademunt

Keyword(s):

Cell Death ◽

Programmed Cell Death ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Neurotrophin Receptor ◽

Finger Protein

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Requirement for the Murine Zinc Finger Protein ZFR in Perigastrulation Growth and Survival

Molecular and Cellular Biology ◽

10.1128/mcb.21.8.2880-2890.2001 ◽

2001 ◽

Vol 21 (8) ◽

pp. 2880-2890 ◽

Cited By ~ 18

Author(s):

Madeleine J. Meagher ◽

Robert E. Braun

Keyword(s):

Cell Death ◽

Programmed Cell Death ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Cellular Growth ◽

Gene Encoding ◽

Growth And Survival ◽

Finger Protein ◽

Development Delay ◽

Cellular Phenotypes

ABSTRACT The transition from preimplantation to postimplantation development leads to the initiation of complex cellular differentiation and morphogenetic movements, a dramatic decrease in cell cycle length, and a commensurate increase in the size of the embryo. Accompanying these changes is the need for the transfer of nutrients from the mother to the embryo and the elaboration of sophisticated genetic networks that monitor genomic integrity and the homeostatic control of cellular growth, differentiation, and programmed cell death. To determine the function of the murine zinc finger protein ZFR in these events, we generated mice carrying a null mutation in the gene encoding it. Homozygous mutant embryos form normal-appearing blastocysts that implant and initiate the process of gastrulation. Mutant embryos form mesoderm but they are delayed in their development and fail to form normal anterior embryonic structures. Loss of ZFR function leads to both an increase in programmed cell death and a decrease in mitotic index, especially in the region of the distal tip of the embryonic ectoderm. Mutant embryos also have an apparent reduction in apical vacuoles in the columnar visceral endoderm cells in the extraembryonic region. Together, these cellular phenotypes lead to a dramatic development delay and embryonic death by 8 to 9 days of gestation, which are independent of p53 function.

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Regulation of epithelial sodium transport by promyelocytic leukemia zinc finger protein

AJP Renal Physiology ◽

10.1152/ajprenal.00573.2007 ◽

2008 ◽

Vol 295 (1) ◽

pp. F18-F26 ◽

Cited By ~ 15

Author(s):

Anikó Náray-Fejes-Tóth ◽

Cary Boyd ◽

Géza Fejes-Tóth

Keyword(s):

Zinc Finger ◽

Zinc Finger Protein ◽

Promyelocytic Leukemia ◽

Negative Regulator ◽

Sodium Reabsorption ◽

Target Cells ◽

Mrna Levels ◽

Na Transport ◽

Promyelocytic Leukemia Zinc Finger ◽

Finger Protein

Aldosterone is the principal regulator of Na homeostasis, and thereby blood pressure. One of the main targets of aldosterone is the epithelial Na channel (ENaC) located in the apical membrane of target cells. Previous studies identified several genes involved in the regulation of ENaC such as SGK1; however, SGK1 knockout mice have only a mild salt-losing phenotype, indicating that further genes must be involved in the action of aldosterone. In our search for further aldosterone-regulated genes, we discovered that aldosterone, at physiological concentrations, induces the expression of the promyelocytic leukemia zinc finger protein (PLZF) in renal cortical collecting duct (CCD) cell lines that stably express mineralocorticoid receptors (MRs). This effect is rapid and does not require de novo protein synthesis, suggesting a direct action. Surprisingly, stable overexpression of human or mouse PLZF isoforms significantly decreased transepithelial Na transport in CCD cells while having no effect on the integrity of the monolayers. In parallel with the decline in Na transport, PLZF suppressed the mRNA levels of β- and γ-ENaC subunits. These observations suggest that PLZF is a negative regulator of ENaC in renal epithelial cells and might be part of a negative feedback loop that limits aldosterone's stimulatory effects on sodium reabsorption.

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The yeast MOT2 gene encodes a putative zinc finger protein that serves as a global negative regulator affecting expression of several categories of genes, including mating-pheromone-responsive genes.

Molecular and Cellular Biology ◽

10.1128/mcb.14.5.3150 ◽

1994 ◽

Vol 14 (5) ◽

pp. 3150-3157 ◽

Cited By ~ 16

Author(s):

K Irie ◽

K Yamaguchi ◽

K Kawase ◽

K Matsumoto

Keyword(s):

Zinc Finger ◽

Zinc Finger Protein ◽

Signal Transduction Pathway ◽

Negative Regulator ◽

Growth Defect ◽

Recessive Mutation ◽

Temperature Sensitive ◽

Pheromone Response Pathway ◽

Finger Protein ◽

Putative Zinc Finger

The STE4 gene encodes the beta subunit of a heterotrimeric G protein that is an essential component of the pheromone signal transduction pathway. To identify downstream component(s) of Ste4, we sought pseudo-revertants that restored mating competence to ste4 mutants. The suppressor mot2 was isolated as a recessive mutation that restored conjugational competence to a temperature-sensitive ste4 mutant and simultaneously conferred a temperature-sensitive growth phenotype. The MOT2 gene encodes a putative zinc finger protein, the deletion of which resulted in temperature-sensitive growth, increased expression of FUS1 in the absence of pheromones, and suppression of a deletion of the alpha-factor receptor. On the other hand, sterility resulting from deletion of STE4 was not suppressed by the mot2 deletion. These phenotypes are similar to those associated with temperature-sensitive mutations in CDC36 and CDC39, which are proposed to encode general negative regulators of transcription rather than factors involved in the pheromone response pathway. Deletion of MOT2 also caused increased transcription of unrelated genes such as GAL7 and PHO84. Overexpression of MOT2 suppresses the growth defect of temperature-sensitive mutations in CDC36 and CDC39. These observations suggest that Mot2 functions as a general negative regulator of transcription in the same processes as Cdc36 and Cdc39.

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Arabidopsis zinc-finger protein 2 is a negative regulator of ABA signaling during seed germination

Journal of Plant Physiology ◽

10.1016/j.jplph.2010.05.010 ◽

2010 ◽

Vol 167 (16) ◽

pp. 1418-1421 ◽

Cited By ~ 13

Author(s):

Gabriele Drechsel ◽

Sabine Raab ◽

Stefan Hoth

Keyword(s):

Seed Germination ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Negative Regulator ◽

Aba Signaling ◽

Finger Protein

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MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP

Biochemical Journal ◽

10.1042/bj20090976 ◽

2010 ◽

Vol 426 (1) ◽

pp. 43-53 ◽

Cited By ~ 99

Author(s):

Craig W. Younce ◽

Pappachan E. Kolattukudy

Keyword(s):

Oxidative Stress ◽

Heart Failure ◽

Cell Death ◽

Er Stress ◽

Zinc Finger ◽

Zinc Finger Protein ◽

Beclin 1 ◽

Finger Protein ◽

Caspase 2 ◽

Specific Inhibitors

MCP-1 (monocyte chemotactic protein-1) plays a critical role in the development of heart failure that is known to involve apoptosis. How MCP-1 contributes to cell death involved in the development of heart disease is not understood. In the present study we show that MCP-1 causes death in cardiac myoblasts, H9c2 cells, by inducing oxidative stress which causes ER stress leading to autophagy via a novel zinc-finger protein, MCPIP (MCP-1-induced protein). MCPIP expression caused cell death, and knockdown of MCPIP attenuated MCP-1induced cell death. It caused induction of iNOS (inducible NO synthase), translocation of the NADPH oxidase subunit phox47 from the cytoplasm to the membrane, production of ROS (reactive oxygen species), and induction of ER (endoplasmic reticulum) stress markers HSP40 (heat-shock protein 40), PDI (protein disulfide-isomerase), GRP78 (guanine-nucleotide-releasing protein 78) and IRE1α (inositol-requiring enzyme 1α). It also caused autophagy, as indicated by beclin-1 induction, cleavage of LC3 (microtubule-associated protein 1 light chain 3) and autophagolysosome formation, and apoptosis, as indicated by caspase 3 activation and TUNEL (terminal deoxynucleotidyltransferase-mediated dUTP nick-end labelling) assay. Inhibitors of oxidative stress, including CeO2 nanoparticles, inhibited ROS formation, ER stress, autophagy and cell death. Specific inhibitors of ER stress inhibited autophagy and cell death as did knockdown of the ER stress signalling protein IRE1. Knockdown of beclin-1 and autophagy inhibitors prevented cell death. This cell death involved caspase 2 and caspase 12, as specific inhibitors of these caspases prevented MCPIP-induced cell death. Microarray analysis showed that MCPIP expression caused induction of a variety of genes known to be involved in cell death. MCPIP caused activation of JNK (c-Jun N-terminal kinase) and p38 and induction of p53 and PUMA (p53 up-regulated modulator of apoptosis). Taken together, these results suggest that MCPIP induces ROS/RNS (reactive nitrogen species) production that causes ER stress which leads to autophagy and apoptosis through caspase 2/12 and IRE1α–JNK/p38–p53–PUMA pathway. These results provide the first molecular insights into the mechanism by which elevated MCP-1 levels associated with chronic inflammation may contribute to the development of heart failure.

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