The Plant Cell (PLANT CELL)

Publisher: American Society of Plant Physiologists; American Society of Plant Biologists, American Society of Plant Biologists

Journal description

The Plant Cell, which is published monthly (one volume per year) by the American Society of Plant Biologists (ASPB), is in its 13th year of publication. Within three years of its initial publication, The Plant Cell ranked first in impact among journals publishing primary research in the plant sciences. It has continued to maintain this standard of excellence ever since. The Plant Cell was founded on four key tenets: (1) to publish the most exciting, cutting-edge research in plant cellular and molecular biology, (2) to provide the most rapid turn-around time possible for reviewing and publishing a research paper, (3) to feature the highest quality reproduction of data, and (4) to provide, in the front section of the journal, a more interactive format for commentaries, opinion pieces, and the exchange of information and ideas in review articles, meeting reports, and insightful overviews of featured research papers. Moreover, our all-review issues, each of which focuses on a specific area of plant biology, are highly regarded teaching and reference tools. Those highlighting Plant-Microbe Interactions and Plant Vegetative Development are available for purchase by individuals.

Current impact factor: 9.34

Impact Factor Rankings

2016 Impact Factor Available summer 2017
2014 / 2015 Impact Factor 9.338
2013 Impact Factor 9.575
2012 Impact Factor 9.251
2011 Impact Factor 8.987
2010 Impact Factor 9.396
2009 Impact Factor 9.293
2008 Impact Factor 9.296
2007 Impact Factor 9.653
2006 Impact Factor 9.868
2005 Impact Factor 11.088
2004 Impact Factor 11.295
2003 Impact Factor 10.679
2002 Impact Factor 10.751
2001 Impact Factor 11.081
2000 Impact Factor 11.093
1999 Impact Factor 10.463
1998 Impact Factor 11.757
1997 Impact Factor 9.709

Impact factor over time

Impact factor

Additional details

5-year impact 10.53
Cited half-life 8.60
Immediacy index 1.71
Eigenfactor 0.08
Article influence 3.47
Website Plant Cell Online, The website
Other titles Plant cell online., The Plant cell
ISSN 1040-4651
OCLC 18424872
Material type Periodical, Internet resource
Document type Journal / Magazine / Newspaper, Internet Resource

Publisher details

American Society of Plant Biologists

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • On author's personal website and institutional repository
    • State that pre-print is under review/accepted
    • Remove pre-print on publication and replace with toll-free link to publisher version
    • If funding agency rules apply, authors may post articles in PubMed Central 12 months after publication
    • Must link to publisher version, toll-free link provided
    • Publisher's version/PDF cannot be used
    • Publisher last reviewed on 25/03/2014
  • Classification

Publications in this journal

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    [Show abstract] [Hide abstract]
    ABSTRACT: C4 photosynthesis in grasses requires the coordinated movement of metabolites through two specialized leaf cell types, mesophyll (M) and bundle sheath (BS) to concentrate CO2 around Rubisco. Despite the importance of transporters in this process, few have been identified or rigorously characterized. In maize, ZmDCT2 has been proposed to function as a plastid-localized malate transporter and is preferentially expressed in BS cells. Here, the role of ZmDCT2 in maize leaves was characterized using Ac-tagged mutant alleles. Our results indicate that ZmDCT2 enables the transport of malate into the BS chloroplast. Isotopic labeling experiments show that the loss of ZmDCT2 resulted in markedly different metabolic network operation and dramatically reduced biomass production. In the absence of a functioning malate shuttle, dct2 mutants survive through the enhanced use of the PEPCK carbon shuttle pathway that in wild-type maize accounts for approximately 25% of the photosynthetic activity. The results emphasize the importance of malate transport during C4 photosynthesis, define the role of a primary malate transporter in BS cells, and support a model for carbon exchange between BS and M cells in maize.
    Preview · Article · Jan 2016 · The Plant Cell
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    ABSTRACT: In the postgenomic era, it is increasingly apparent that the one gene-one function model is not sufficiently broad to fully understand the molecular mechanisms at play within a cell. Numerous levels of complexity, such as protein-protein interactions and posttranslational modifications, were shown to be essential in determining the role, localization, and activity of a protein. A frequently studied modification is ubiquitination, the covalent binding of the small protein modifier ubiquitin to a target protein. Multiple reports provide useful insights into the plant 'ubiquitinome', but mostly at the protein level without comprehensive site identification. Here, we implemented a new technology, ubiquitin combined fractional diagonal chromatography (COFRADIC), for proteome-wide ubiquitination site mapping on Arabidopsis thaliana cell cultures. We identified 3,009 sites on 1,607 proteins, thereby greatly increasing the number of known ubiquitination sites in this model plant. Finally, the Ubiquitination Site tool provided gives access to the obtained ubiquitination sites, not only to consult the ubiquitination status of a given protein, but also to conduct intricate experiments aiming to study the roles of specific ubiquitination events. Together with the antibodies recognizing the ubiquitin remnant motif, ubiquitin COFRADIC represents a powerful tool to resolve the ubiquitination maps of numerous cellular processes in plants.
    No preview · Article · Jan 2016 · The Plant Cell
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    Preview · Article · Jan 2016 · The Plant Cell
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    ABSTRACT: Here, we show that the Nitrate Regulatory Gene 2 (NRG2), a novel gene identified using forward genetics, mediates nitrate signaling in Arabidopsis. The mutation in NRG2 disrupted the induction of nitrate-responsive genes after nitrate treatment by an ammonium-independent mechanism. The nitrate content in roots was lower in the mutants than in WT, which may have resulted from reduced expression of NRT1.1 (NPF6.3, a nitrate transporter/receptor) and up-regulation of NRT1.8 (NPF7.2, a xylem nitrate transporter). Genetic and molecular data suggest that NRG2 functions upstream of NRT1.1 in nitrate signaling. Furthermore, NRG2 directly interacts with the nitrate regulator NLP7 in the nucleus, but nuclear retention of NLP7 in response to nitrate is not dependent on NRG2. Transcriptomic analysis revealed that genes involved in four nitrogen-related clusters including nitrate transport and response to nitrate were differentially expressed in the nrg2 mutants. A nitrogen compound transport cluster containing some members of the NRT/PTR family was regulated by both NRG2 and NRT1.1, while no nitrogen-related clusters showed regulation by both NRG2 and NLP7. Thus, NRG2 plays a key role in nitrate regulation in part through modulating NRT1.1 expression and may function with NLP7 via their physical interaction.
    Preview · Article · Jan 2016 · The Plant Cell
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    ABSTRACT: Nuclear-localized RNA binding proteins are involved in various aspects of RNA metabolism, which in turn modulates gene expression. However, the functions of nuclear-localized RNA binding proteins in plants are poorly understood. Here we report the functions of two proteins containing RNA recognition motifs, At RZ-1B and At RZ-1C, in Arabidopsis. At RZ-1B and At RZ-1C were localized to nuclear speckles and interacted with a spectrum of serine/arginine-rich (SR) proteins through their C-termini. At RZ-1C preferentially bound to purine-rich RNA sequences in vitro through its N-terminal RNA recognition motif. Disrupting the RNA-binding activity of At RZ-1C with SR proteins through over-expression of the C-terminus of At RZ-1C conferred defective phenotypes similar to those observed in At rz-1b/At rz-1c double mutants, including delayed seed germination, reduced stature, and serrated leaves. Loss of function of At RZ-1B and At RZ-1C was accompanied by defective splicing of many genes and global perturbation of gene expression. In addition, we found that At RZ-1C directly targeted FLC, promoting efficient splicing of FLC introns and repressing FLC transcription. Our findings highlight the critical role of At RZ-1B/1C in regulating RNA splicing, gene expression, and many key aspects of plant development via interaction with proteins including SR proteins.
    No preview · Article · Dec 2015 · The Plant Cell
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    ABSTRACT: Digalactosyldiacylglycerol synthase 1 (DGDl) is a chloroplast outer-membrane protein responsible for the synthesis of digalactosyldiacylglycerol (DGDG) from monogalactosyldiacylglycerol (MGDG). The dgd1 mutants have a greater than 90% reduction in DGDG content, reduced photosynthesis, and altered chloroplast morphology. However, the most pronounced visible phenotype is the extremely short inflorescence stem, but how deficient DGDG synthesis causes this phenotype is not known. We found that, in dgd1 mutants, phloem cap cells were lignified and jasmonic acid (JA)-responsive genes highly upregulated under normal growth conditions. The coi1 (coronative insensitive1) dgd1 and aos (allene oxide synthase) dgd1 double mutants no longer exhibited the short-inflorescence-stem and lignification phenotypes but still had the same lipid profile and reduced photosynthesis as dgd1 single mutants. Hormone and lipidomics analyses showed higher levels of JA, JA-isoleucine, 12-oxo-phytodienoic acid (OPDA) and Arabidopsides in dgd1 mutants. Transcript and protein levels analyses further suggest that JA biosynthesis in dgd1 is initially activated through increased expression of genes encoding 13-lipoxygenases (LOXs) and phospholipase A-Iγ3 (At1g51440), a plastid lipase with a high substrate preference for MGDG, and sustained by further increase in LOX and allene oxide cyclase mRNA and protein levels. Our results demonstrate a link between the synthesis of DGDG and JA.
    Preview · Article · Dec 2015 · The Plant Cell
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    ABSTRACT: MSI1 belongs to a family of histone-binding WD40-repeat proteins. In Arabidopsis thaliana, there are five genes encoding MSI1-like proteins but their functions in diverse chromatin-associated complexes are poorly understood. Here, we show that MSI1 is part of a histone deacetylase complex. We co-purified histone deacetylase 19 (HDA19) with MSI1 and SIN3-like proteins and provide evidence that MSI1 and HDA19 associate into the same complex in vivo. These data suggest that MSI1, HDA19 and histone deacetylation complex1 (HDC1) protein form a core complex that can integrate various SIN3-like proteins. We found that reduction of MSI1 or HDA19 causes upregulation of ABA receptor genes and hypersensitivity of ABA-responsive genes. The MSI1-HDA19 complex fine-tunes ABA signaling by binding to the chromatin of ABA receptor genes and by maintaining low levels of H3K9ac, thereby affecting the expression level of ABA receptors. Reduced MSI1 or HDA19 levels led to increased tolerance to salt stress corresponding to the increased ABA sensitivity of gene expression. Together, our results show the presence of a MSI1-HDA19 complex that fine-tunes ABA signaling in Arabidopsis.
    No preview · Article · Dec 2015 · The Plant Cell
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    Preview · Article · Dec 2015 · The Plant Cell
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    ABSTRACT: Vegetative phase change in flowering plants is regulated by a decrease in the level of miR156. The molecular mechanism of this temporally regulated decrease in miR156 expression is still unknown. Most of the miR156 in Arabidopsis shoots is produced by MIR156A and MIR156C. We found that the down-regulation of these genes during vegetative phase change is associated with an increase in their level of histone H3 lysine 27 trimethylation (H3K27me3), and requires this chromatin modification. The increase in H3K27me3 at MIR156A/MIR156C is associated with an increase in the binding of PRC2 to these genes, and is mediated redundantly by the E(z) homologs, SWINGER (SWN) and CURLY LEAF (CLF). The CHD3 chromatin remodeler, PICKLE (PKL), promotes the addition of H3K27me3 to MIR156A/MIR156C, but is not responsible for the temporal increase in this chromatin mark. PKL is bound to the promoters of MIR156A/MIR156C, where it promotes low levels of H3K27ac early in shoot development, and stabilizes the nucleosome at the +1 position. These results suggest a molecular m.
    No preview · Article · Dec 2015 · The Plant Cell
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    Preview · Article · Dec 2015 · The Plant Cell
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    Preview · Article · Dec 2015 · The Plant Cell

  • No preview · Article · Dec 2015 · The Plant Cell