Journal of Cell Science (J Cell Sci)

Publisher: Company of Biologists, Company of Biologists

Journal description

Journal of Cell Science covers the complete range of topics in cell biology and is also of key interest to developmental biologists, molecular biologists and geneticists. It is one of the leading journals in the field, and its impact factor is rising steadily. Each issue includes research articles, as well as review articles commissioned from experts in particular fields, brief syntheses of important areas and topical comment. Journal of Cell Science is published twice monthly (24 issues/year).

Current impact factor: 5.43

Impact Factor Rankings

2016 Impact Factor Available summer 2017
2014 / 2015 Impact Factor 5.432
2013 Impact Factor 5.325
2012 Impact Factor 5.877
2011 Impact Factor 6.111
2010 Impact Factor 6.29
2009 Impact Factor 6.144
2008 Impact Factor 6.247
2006 Impact Factor 6.427
2005 Impact Factor 6.543
2004 Impact Factor 6.91
2003 Impact Factor 7.25
2002 Impact Factor 6.954
2001 Impact Factor 6.213
2000 Impact Factor 5.996
1999 Impact Factor 6.044
1998 Impact Factor 5.453
1997 Impact Factor 5.081
1996 Impact Factor 4.935
1995 Impact Factor 4.827
1994 Impact Factor 4.336
1993 Impact Factor 3.432
1992 Impact Factor 3.593

Impact factor over time

Impact factor

Additional details

5-year impact 6.00
Cited half-life 8.80
Immediacy index 0.93
Eigenfactor 0.09
Article influence 2.53
Website Journal of Cell Science website
Other titles Journal of cell science (Online), Journal of cell science
ISSN 1477-9137
OCLC 37637228
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Company of Biologists

  • Pre-print
    • Author cannot archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • On author's personal website immediately
    • If mandated by a funding agency or institution, the author's post-print may be deposited in designated repository after a 12 months embargo period or as mandated
    • Authors retain copyright
    • Publisher's version/PDF cannot be used
    • Must link to publisher version
    • Publisher will deposit the final publisher version in PMC for authors funded by RCUK, HHMI, NIH, MRC, Wellcome Trust for release 6 or 12 months after publication (as mandated) or immediately upon payment of fee.
    • Non-commercial use
  • Classification

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: The accumulation of ubiquitinated proteinaceous inclusions represents a complex process, reflecting the disequilibrium between aggregate formation and aggregate clearance. Although decreasing aggregate formation or augmenting aggregate clearance will ultimately lead to diminished aggregate-burden, in terms of disease pathogenesis, the different approaches can have distinct outcomes. Using a novel cell based assay that can distinguish newly formed versus preformed inclusions, we demonstrate that two proteins previously implicated in the autophagic clearance of expanded polyglutamine inclusions, HspB7 and Alfy, actually affect very distinct cellular processes to affect aggregate-burden. Using this cell-based assay we also establish that constitutive expression of the aggregation prone protein can measurably slow the elimination of protein aggregates, since not all aggregates appear to be available for degradation. This new assay can therefore not only determine at what step a modifier may impact aggregate burden, but also can be used to provide new insight into how protein aggregates are targeted for degradation.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Nonsense-mediated mRNA decay (NMD) is an mRNA quality-control mechanism that typifies all eukaryotes examined to date. NMD surveys newly synthesized mRNAs and degrades those that harbor a premature termination codon (PTC), thereby preventing the production of truncated proteins that could result in disease in humans. This is evident from dominantly inherited diseases that are due to PTC-containing mRNAs that escape NMD. Although many cellular NMD targets derive from mistakes made during, for example, pre-mRNA splicing and, possibly, transcription initiation, NMD also targets ∼10% of normal physiological mRNAs so as to promote an appropriate cellular response to changing environmental milieus, including those that induce apoptosis, maturation or differentiation. Over the past ∼35 years, a central goal in the NMD field has been to understand how cells discriminate mRNAs that are targeted by NMD from those that are not. In this Cell Science at a Glance and the accompanying poster, we review progress made towards this goal, focusing on human studies and the role of the key NMD factor up-frameshift protein 1 (UPF1).
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Ciliary axonemes and basal bodies were present in the last eukaryotic common ancestor and play critical roles in sensing and responding to environmental cues. Peptidergic signaling, generally considered a metazoan innovation, is essential for organismal development and homeostasis. Peptidylglycine alpha-amidating monooxygenase (PAM) is crucial for the last step of bioactive peptide biosynthesis. However, identification of a complete PAM-like gene in green algal genomes suggests ancient evolutionary roots for bioactive peptide signaling. We demonstrate that the Chlamydomonas reinhardtii PAM gene encodes an active peptide amidating enzyme (CrPAM) that shares key structural and functional features with the mammalian enzyme, indicating that components of the peptide biosynthetic pathway predate multicellularity. In addition to its secretory pathway localization, CrPAM localizes to cilia and tightly associates with the axonemal superstructure, revealing a novel axonemal enzyme activity. This localization pattern is conserved in mammals, with PAM present in both motile and immotile sensory cilia. The conserved ciliary localization of PAM adds to the known signaling capabilities of the eukaryotic cilium and provides a potential mechanistic link between peptidergic signaling and endocrine abnormalities commonly observed in ciliopathies.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Understanding the function of cellular machines requires a thorough analysis of the structural elements that underline their function. Electron microscopy (EM) has been pivotal in providing information about cellular ultrastructure, as well as macromolecular organization. Biological materials can be physically fixed by vitrification and imaged with cryo-electron tomography (cryo-ET) in a close-to-native condition. Using this technique, one can acquire three-dimensional (3D) information about the macromolecular architecture of cells, depict unique cellular states and reconstruct molecular networks. Technical advances over the last few years, such as improved sample preparation and electron detection methods, have been instrumental in obtaining data with unprecedented structural details. This presents an exciting opportunity to explore the molecular architecture of both individual cells and multicellular organisms at nanometer to subnanometer resolution. In this Commentary, we focus on the recent developments and in situ applications of cryo-ET to cell and structural biology.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: During angiogenesis, endothelial cells must coordinate matrix proteolysis with migration. We tested here whether the focal adhesion scaffold protein Hic-5 regulated endothelial sprouting in three-dimensions. Hic-5 silencing reduced endothelial sprouting and lumen formation, and sprouting defects were rescued by the return of Hic-5 expression. Pro-angiogenic factors enhanced co-localization and complex formation between membrane type-1 matrix metalloproteinase (MT1-MMP) and Hic-5, but not paxillin, and the LIM2 and LIM3 domains of Hic-5 were necessary and sufficient for MT1-MMP complex formation. MT1-MMP and Hic-5 complex formation and localization within detergent-resistant membrane fractions were enhanced during endothelial sprouting, and Hic-5 depletion lowered surface levels of MT1-MMP. In addition, we observed that loss of Hic-5 partially reduced MT1-MMP and focal adhesion kinase (FAK) complex formation, suggesting that Hic-5 bridges MT1-MMP and FAK. Finally, Hic-5 LIM2-3 deletion mutants reduced sprout initiation. Hic-5, MT1-MMP, and FAK co-localized in angiogenic vessels during porcine pregnancy, supporting that this complex assembles during angiogenesis in vivo. Collectively, Hic-5 appears to enhance complex formation between MT1-MMP and FAK in activated endothelial cells, which likely coordinates matrix proteolysis and cell motility.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Ten-eleven translocation (TET) proteins are key players involved in the dynamic regulation of cytosine methylation and demethylation. Inactivating mutations of TET2 are frequently found in human malignancies, highlighting the essential role of TET2 in cellular transformation. However, the factors that control TET enzymatic activity remain largely unknown. Here we found that MBD3 and its analogue MBD3L2 can specifically modulate the enzymatic activity of Tet2 protein, but not Tet1 and Tet3 proteins, in converting 5mC into 5hmC. Moreover, MBD3L2 is more effective than MDB3 in promoting Tet2 enzymatic activity via strengthening the binding affinity between Tet2 and the methylated DNA target. Further analysis revealed pronounced decreases in 5mC levels at MBD3L2 and Tet2 co-occupied genomic regions, most of which are promoter elements associated with either cancer-related genes or genes involved in the regulation of cellular metabolic processes. Our data add new insights into the regulation of Tet2 activity by MBD3 and MBD3L2 in modulating its target gene activities in cancer development and have important applications in understanding how dysregulation of TET2 may contribute to human malignancy.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Bi-directional non-coding transcripts and their ∼29 nt small RNA products are known to guide DNA deletion in Tetrahymena, leading to the removal of one-third of the genome from developing somatic nuclei. Using an antibody specific for long double-stranded RNAs (dsRNAs), we determined the dynamic subcellular distributions of these RNAs. Conjugation-specific dsRNAs are found and show sequential appearances in parental germline, parental somatic nuclei and finally in new somatic nuclei of progeny. The dsRNAs in germline nuclei and new somatic nuclei are likely transcribed from the sequences destined for deletion; however, the dsRNAs in parental somatic nuclei are unexpected, and PCR analyses suggest their transcription in this nucleus. Deficiency in RNAi pathway leads to abnormal aggregations of dsRNA in both the parental and new somatic nuclei, whereas accumulation of dsRNAs in the germline nuclei is only seen in the Dicer-like gene mutant. In addition, RNAi mutants display an early loss of dsRNAs from developing somatic nuclei. Thus, long dsRNAs are made in multiple nuclear compartments and some are linked to small RNA production whereas others may participate in their regulations.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Degradation of cellular material by autophagy is essential for cell survival and homeostasis, and requires intracellular transport of autophagosomes to encounter acidic lysosomes through unknown mechanisms. Here we identify the PX domain-containing kinesin Klp98A as a novel regulator of autophagosome formation, transport and maturation in Drosophila. Depletion of Klp98A caused abnormal clustering of autophagosomes and lysosomes at the cell center and reduced the formation of starvation-induced autophagic vesicles. Reciprocally, overexpression of Klp98A redistributed autophagic vesicles toward the cell periphery. These effects were accompanied by reduced autophagosome-lysosome fusion and autophagic degradation. In contrast, depletion of the conventional kinesin heavy chain caused a similar mislocalization of autophagosomes without perturbing their fusion with lysosomes, indicating that vesicle fusion and localization are separable, independent events. Klp98A-mediated fusion required the endolysosomal GTPase Rab14, which interacted and colocalized with Klp98A and required Klp98A for normal localization. Thus, Klp98A coordinates the movement and fusion of autophagic vesicles by regulating their positioning and interaction with the endolysosomal compartment.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Pannexin 3 (Panx3) and connexin 43 (Cx43) are two major gap junction proteins expressed in osteoblasts. Here, we studied their functional relationships in skeletal formation by generating Panx3(-/-) and Panx3(-/-);Cx43(-/-) mice and comparing their skeletal phonotypes with Cx43(-/-) mice. Panx3(-/-) mice displayed defects in endochondral and intramembranous ossification, resulting in severe dwarfism and reduced bone density. The skeletal abnormalities of Panx3(-/-);Cx43(-/-) mice were similar to those in Panx3(-/-) mice. The gross appearance of newborn Cx43(-/-) skeletons showed no obvious abnormalities except for less mineralization of the skull. In Panx3(-/-) mice, proliferation of chondrocytes and osteoblasts increased and differentiation of these cells was inhibited. Panx3 promoted expression of osteogenic genes such as ALP, Ocn, and Cx43 by regulating Osx expression. Panx3 was induced in the early differentiation stage and reduced in the maturation stage of osteoblasts when Cx43 expression increased for mineralization. Furthermore, only Panx3 functioned as an ER Ca(2+) channel to promote differentiation, and it could rescue mineralization defects in Cx43(-/-) calvarial cells. Our findings revealed that Panx3 and Cx43 have distinct functions in skeletal formation.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: How mechanical cues from the extracellular environment are translated biochemically to modulate the effects of TGF-β on myofibroblast differentiation remains a critical area of investigation. We report here that the focal adhesion protein, Hic-5, is required for the mechanically dependent generation of stress fibers in response to TGF-β. Successful generation of stress fibers promotes the nuclear localization of the transcriptional cofactor MRTF-A and this correlates with the mechanically dependent induction of α-SMA and Hic-5 in response to TGF-β. As a consequence of regulating stress fiber assembly, Hic-5 is required for the nuclear accumulation of MRTF-A, and the induction of α-SMA as well as cellular contractility, suggesting a critical role for Hic-5 in myofibroblast differentiation. Indeed, the expression of Hic-5 was transient in acute wounds and persistent in pathogenic scars, and co-localized with α-SMA expression in vivo. Together, these data suggest that a mechanically dependent feed forward loop, elaborated by the reciprocal regulation of MRTF-A localization by Hic-5 and Hic-5 expression by MRTF-A, plays a critical role in myofibroblast differentiation in response to TGF-β.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: Pluripotent embryonic stem (ES) cells are characterized by their capacity to self-renew indefinitely while maintaining the potential to differentiate into all cell types of an adult organism. Both the undifferentiated and differentiated states are defined by specific gene expression programs that are regulated at the chromatin level. By employing the KDM6-specific GSK-J4 inhibitor and by targeted gene knockout/knockdown (KO/KD), we have analyzed the contribution of the H3K27me2,3-specific demethylases KDM6A and KDM6B to murine ES cell differentiation. We observe that inhibition of the H3K27 demethylase activity induces DNA damage along with activation of the DNA damage response (DDR) and cell death in differentiating but not in undifferentiated ES cells. Laser microirradiation experiments revealed that the H3K27me3 mark but not the KDM6B protein co-localize with γH2AX+ sites of DNA damage in differentiating ES cells. Lack of H3K27me3 attenuates the GSK-J4-induced DDR in differentiating Eed KO ES cells. Collectively our findings indicate that differentiating ES cells depend on KDM6 and that the H3K27me3 demethylase activity is critically involved in DDR and survival of differentiating ES cells.
    No preview · Article · Jan 2016 · Journal of Cell Science
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    ABSTRACT: The kinesin KIF17 localizes at MT plus-ends and contributes to regulation of MT stabilization, and epithelial polarization. We now show that KIF17 localizes at cell-cell adhesions and that KIF17 depletion inhibits accumulation of actin at the apical pole of cells grown in 3D organotypic cultures and alters the distribution of actin and E-cadherin in cells cultured in 2D on solid supports. Overexpression of full-length KIF17 constructs or truncation mutants containing the N-terminal motor domain resulted in accumulation of newly incorporated GFP-actin into junctional actin foci, cleared E-cadherin from cytoplasmic vesicles and stabilized cell-cell adhesions to challenge with calcium depletion. Expression of these KIF17 constructs also increased cellular levels of active RhoA, while active RhoA was diminished in KIF17-depleted cells. Inhibition of Rho or its effector ROCK, or expression of LIMK1 kinase-dead or activated cofilin(S3A) inhibited KIF17-induced junctional actin accumulation. Interestingly, KIF17 activity toward actin depends on the motor domain but is independent of MT binding. Together, these data show that KIF17 can modify Rho-GTPase signaling to influence junctional actin and the stability of the apical junctional complex of epithelial cells.
    No preview · Article · Jan 2016 · Journal of Cell Science