Journal of Cell Science Impact Factor & Information

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: 5.33

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 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
Year

Additional details

5-year impact 6.38
Cited half-life 8.00
Immediacy index 1.03
Eigenfactor 0.11
Article influence 2.89
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.
    • On a non-profit server
  • Classification
    ​ blue

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Myelin is comprised of a compactly stacked massive surface area of protein-poor, thick membrane that insulates axons to allow fast signal propagation. Increasing levels of the myelin protein plasmolipin (PLLP) were correlated with post-natal myelination. However its function is unknown. Here, the intracellular localization and dynamics of PLLP was characterized in primary glial and cultured cells using fluorescent protein (FP) tagged PLLP and anti-PLLP antibodies. PLLP localized to and recycled between the plasma membrane (PM) and the Golgi apparatus. In the Golgi apparatus PLLP forms oligomers based on fluorescence resonance energy transfer (FRET). PLLP oligomers blocked Golgi to PM transport of the secretory protein VSVG, but not a VSVG mutant with an elongated transmembrane domain. Laurdan staining analysis showed that this block is associated with PLLP-induced proliferation of liquid-ordered membranes. These findings show the capacity of PLLP to assemble potential myelin membrane precursor domains at the Golgi apparatus via its oligomerization and attraction of liquid ordered lipids. These data support a model whereby PLLP functions in myelin biogenesis by organization of myelin liquid ordered membranes in the Golgi apparatus. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.166249
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    ABSTRACT: Intracellular beta amyloid (Aβ) accumulation is a key feature of early Alzheimer's disease (AD) and precedes the appearance of Aβ in extracellular plaques. Aβ is generated through proteolytic processing of amyloid precursor protein (APP), but the intracellular site of Aβ production is unclear. APP has been localized to multivesicular endosomes/bodies (MVBs) where sorting of APP onto ILVs could promote amyloidogenic processing or reduce Aβ production/accumulation by sorting APP and processing products to lysosomes for degradation. We show that APP localizes to the ILVs of a subset of MVBs that also traffic EGF receptor (EGFR), and is delivered to lysosomes for degradation. Depletion of the ESCRT components, Hrs or Tsg101, inhibited targeting of APP to ILVs and the subsequent delivery to lysosomes and lead to increased intracellular Aβ accumulation. This was accompanied by dramatically decreased Aβ secretion. Thus, the early ESCRT machinery has a dual role in limiting intracellular Aβ accumulation through targeting of APP and processing products to the lysosome for degradation and promoting Aβ secretion. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.170233
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    ABSTRACT: TM9 proteins (also named Phg1 proteins) have been previously shown to control cell adhesion by determining the cell surface localization of adhesion proteins such as the Dictyostelium SibA protein. Here we show that the glycine-rich transmembrane domain (TMD) of SibA is sufficient to confer to a reporter protein Phg1A-dependent surface targeting. Accordingly, in Dictyostelium phg1A KO cells, proteins with glycine-rich TMDs are less efficiently transported out of the endoplasmic reticulum (ER) and to the cell surface. Phg1A, as well as its human ortholog TM9SF4 specifically associate with glycine-rich TMDs. In human cells, genetic inactivation of TM9SF4 results in an increased retention of glycine-rich TMDs in the endoplasmic reticulum, while TM9SF4 overexpression enhances their surface localization. The bulk of the TM9SF4 protein is localized in the Golgi apparatus where a proximity-ligation assay suggests that it may interact with glycine-rich TMDs. Together, these results suggest that one of the main roles of TM9 proteins is to serve as intramembrane cargo receptors controlling exocytosis and surface localization of a subset of membrane proteins. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.164848
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    ABSTRACT: Alzheimer's disease (AD) is characterized by amyloid-β (Aβ) peptide accumulation in the brain. CALHM1, a cell-surface Ca(2+) channel expressed in brain neurons, has anti-amyloidogenic properties in cell cultures. Here, we show that CALHM1 controls Aβ levels in vivo in the mouse brain through a previously unrecognized mechanism of regulation of Aβ clearance. Using pharmacological and genetic approaches in cell lines, we found that CALHM1 ion permeability and extracellular Ca(2+) were required for the Aβ lowering effect of CALHM1. Aβ level reduction by CALHM1 could be explained by an increase in extracellular Aβ degradation by insulin-degrading enzyme (IDE), extracellular secretion of which was robustly potentiated by CALHM1 activation. Importantly, Calhm1 knockout in mice reduced IDE enzymatic activity in the brain, and increased up to ∼50% endogenous Aβ concentrations in both the whole brain and primary neurons. Thus, CALHM1 controls Aβ levels in cell lines and in vivo by facilitating neuronal and Ca(2+)-dependent degradation of extracellular Aβ by IDE. This work identifies CALHM1 ion channel as a potential target for promoting amyloid clearance in AD. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.167270
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    ABSTRACT: Here we describe a high content microscopy-based screen that allowed us to systematically assess and rank proteins involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport in mammalian cells. Using a cell line stably expressing a GFP-tagged Golgi enzyme, we used brefeldin A treatment to stimulate the production of Golgi-to-ER carriers and then quantitatively analyse populations of cells for changes in this trafficking event. Systematic RNA interference-based depletion of 58 Rab GTPase proteins and 12 Rab-accessory proteins of the PRAF, YIPF and YIF protein families revealed 9 of these as strong regulators. In addition to demonstrating roles for Rab1, Rab2 and Rab6a/a' in this transport step, we also identified Rab10 and Rab11a as playing a role and being physically present on a proportion of the Golgi-to-ER tubular intermediates. Combinatorial depletions of Rab proteins also revealed previously undescribed functional co-operation and physical co-occurrence between several Rabs. Our approach therefore provides a novel and robust strategy for a more complete investigation of the molecular components required to regulate Golgi-to-ER transport in mammalian cells. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.167973
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    ABSTRACT: Membrane fusion at the vacuole depends on a conserved machinery that includes SNAREs, the Rab7 homolog Ypt7 and its effector HOPS. Here, we demonstrate that Ypt7 has an unexpected additional function by controlling membrane homeostasis and nutrient-dependent signaling on the vacuole surface. We show that Ivy1, the yeast homolog of mammalian missing-in-metastasis (MIM), is a vacuolar effector of Ypt7-GTP, and interacts with the EGO/ragulator complex, an activator of the target of rapamycin kinase complex (TORC1) on vacuoles. Loss of Ivy1 does not affect EGO vacuolar localization and function. In combination with a deletion of individual subunits of the V-ATPase, however, we observed reduced TORC1 activity and massive enlargement of the vacuole surface. Consistent with this, Ivy1 localizes to invaginations at the vacuole surface and on liposomes in a phosphoinositide and Ypt7-GTP-controlled manner, which suggests a role in microautophagy. Our data thus reveal Ivy1 as a novel regulator of vacuole membrane homeostasis with connections to TORC1 signaling. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.164905
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    ABSTRACT: Murine embryonic stem (ES) cells treated with all-trans retinoic acid (RA) differentiate into a homogenous population of glutamatergic neurons. While differentiation is initiated by activation of target genes by the RA-receptors, the downstream transcription factors specifying neuronal fate are less well characterised. We show that transcription factor Pou3f2 (Brn2) is essential for the neuronal differentiation programme. By integrating RNA-seq following Brn2 silencing with Brn2 ChIP-seq, we identify a set of Brn2 target genes required for the neurogenic programme. Further integration of Brn2 ChIP-seq data from RA-treated ES and P19 cells with ES cells differentiated into neuronal precursors by Fgf2 treatment and fibroblasts trans-differentiated into neurons by ectopic Brn2 expression showed Brn2 occupancy of a distinct but overlapping set of genomic loci. However, a set of common binding sites and target genes define the core of the Brn2-regulated neuronal program amongst which is transcription factor Zic1. ShRNA mediated silencing of Zic1 abrogates neural fate thus defining a hierarchical Brn2-Zic1 axis essential to specify the neural fate of RA-treated ES cells. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.168849
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    ABSTRACT: Pyruvate dehydrogenase kinases (PDKs) modulate energy homeostasis in multiple tissues/cell types, under various nutrient conditions, through phosphorylation of the α subunit (PDHE1α) of the pyruvate dehydrogenase (PDH) complex. However, the roles of PDKs in meiotic maturation are currently unknown. Here, by employing morpholino knockdown and overexpression analysis of PDK paralogs (PDK1-4) in mouse oocytes, we established the site-specificity of PDKs toward the phosphorylation of three serine residues (Ser232, Ser293 and Ser300) on PDHE1α. We found that PDK3-mediated phosphorylation of Ser293-PDHE1α results in disruption of meiotic spindle morphology and chromosome alignment and decreased total ATP levels, probably through inhibition of PDH activity. Unexpectedly, we discovered that PDK1/2 promote meiotic maturation as their knockdown disturbs the assembly of meiotic apparatus, without significantly altered ATP content. Moreover, phosphorylation of Ser232-PDHE1α was demonstrated to mediate PDK1/2 action in meiotic maturation, possibly through a mechanism that is distinct from PDH inactivation. These findings reveal divergent roles of PDKs during oocyte maturation and indicate a novel mechanism controlling meiotic structure. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.167049
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    ABSTRACT: We previously described that high luminal calcium in the renal collecting duct attenuates short-term vasopressin-induced aquaporin-2 (AQP2) trafficking via activation of the Calcium-Sensing Receptor (CaSR). Here we evaluated AQP2 phosphorylation and permeability in renal HEK-293 cells and in dissected inner medullary collecting duct, in response to specific activation of CaSR with NPS-R568. In CaSR transfected cells, CaSR activation drastically reduced basal AQP2-pS256 levels thus having an opposite effect with respect to vasopressin action. When forskolin stimulation was performed in the presence of NPS-R568, the increase in AQP2-pS256 and in the osmotic water permeability were prevented. In freshly isolated inner mouse medullar collecting duct stimulation with forskolin in the presence of NPS-R568 prevented the increase in AQP2-pS256 and osmotic water permeability. Our data demonstrate that the activation of CaSR in the collecting duct prevents cAMP-dependent increase in AQP2-pS256 and water permeability, counteracting short-term vasopressin response. By extension, our results bring to the attractive concept that CaSR expressed in distinct nephron segments exerts a negative feedback on hormones acting through the cAMP, conferring high sensitivity of hormone to extracellular calcium. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.168096
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    ABSTRACT: F-BAR proteins are known to participate in cytokinesis, but their mechanisms are not well understood. Here we investigated Rga7p an S. pombe F-BAR protein with a RhoGAP domain. Localization of Rga7p to the cytokinetic cleavage furrow depends on its F-BAR domain, actin filaments, formins Cdc12p and For3p, and the presence of a contractile ring. Rga7p is not required for the constriction of the contractile ring but does participate in the transport of a β-glucan synthetase Bgs4p from the late Golgi compartments to the plasma membrane adjacent to the contractile ring. Cells without Rga7p moved Bgs4p normally from the poles to the Golgi apparatus near the cell center, but Bgs4p then moved slowly from the late Golgi compartments to the cleavage site. The late arrival and lower than normal numbers of Bgs4p result in septal defects late in cytokinesis and lysis of separating cells similar to cells with the mutations in the cwg1(+) gene encoding Bgs4p. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.162974
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    ABSTRACT: Epithelial apicobasal polarity has fundamental roles in epithelial physiology and morphogenesis. The PAR complex, comprising PAR-3, PAR-6 and aPKC, is involved in determining cell polarity in various biological contexts, including in epithelial cells. However, it is not fully understood how the PAR complex induces apicobasal polarity. In this study, we show that PAR-3 regulates the protein expression of Girdin (GIV/CCDC88A), a guanine nucleotide exchange factor (GEF) for heterotrimeric Gαi subunits, at the transcriptional level by cooperating with the AP-2 transcription factor. In addition, we confirmed that PAR-3 physically interacts with Girdin, and show that Girdin, together with the Gαi3, controls tight junction formation, apical domain development and actin organization downstream of PAR-3. Taken together, our findings suggest that transcriptional upregulation of Girdin and Girdin-Gαi3 signaling play crucial roles in regulating epithelial apicobasal polarity via the PAR complex. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.160879
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    ABSTRACT: Antigen presenting cells have the remarkable capacity to transfer exogenous antigens to the cytosol for processing by proteasomes and subsequent presentation on MHC-I molecules, a process termed cross-presentation. It is the target of biomedical approaches that aim to trigger a therapeutic immune response. The receptor-binding B-subunit of Shiga toxin (STxB) is developed as an antigen delivery tool for such immunotherapy applications. In this study, we have analyzed pathways and trafficking factors that are involved in this process. A covalent conjugate between STxB and saporin was generated to quantitatively sample the membrane translocation step to the cytosol in differentiated monocyte-derived THP-1 cells. We have found that retrograde trafficking to the Golgi apparatus was not required for STxB-saporin translocation to the cytosol or for STxB-dependent antigen cross-presentation. Depletion of endosomal Rab7 inhibited, and lowering membrane cholesterol levels favored STxB-saporin translocation. Interestingly, experiments with reducible and non-reducible linker arm STxB conjugates led to the conclusion that after translocation, STxB remained associated with the cytosolic membrane leaflet. In summary, we report novel facets of the endosomal escape process bearing relevance to antigen cross-presentation. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.169383
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    ABSTRACT: All Hedgehog morphogens are released from producing cells, despite being synthesized as N- and C-terminally lipidated molecules, a modification that firmly tethers them to the cell membrane. We previously showed that proteolytic removal of both lipidated peptides, called shedding, releases bioactive Sonic hedgehog (Shh) morphogens from the surface of transfected Bosc23 cells. Using in vivo knockdown together with in vitro cell culture studies, we now show that glypican heparan sulfate (HS) proteoglycans regulate this process through their HS chains in a cell autonomous manner. HS specifically modifies Shh processing at the cell surface, and purified glycosaminoglycans enhance the proteolytic removal of N- and C-terminal Shh peptides under cell-free conditions. The most likely explanation for these observations is direct Shh processing in the extracellular compartment, suggesting that HS acts as a scaffold or activator for Shh ligands and the factors required for their turnover. We also show that purified HS isolated from specific cell types and tissues releases bioactive Shh from pancreatic cancer cells, revealing a previously unknown regulatory role for these versatile molecules in a pathological context. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.170670
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    ABSTRACT: In this study, we elucidated the architectures of two multisubunit complexes, BBSome and Exocyst, through a novel application of fluorescent fusion proteins. By processing lysates from cells co-expressing GFP- and RFP-fusion proteins for immunoprecipitation with anti-GFP Nanobody, protein-protein interactions could be reproducibly visualized by directly observing the immunoprecipitates under a microscope, and evaluated using a microplate reader, without requiring immunoblotting. Using this "visible" immunoprecipitation (VIP) assay, we mapped binary subunit interactions of the BBSome complex, and determined hierarchies of up to four subunit interactions. We also demonstrated the assembly sequence of the BBSome around the centrosome, and showed that BBIP10/BBS18 serves as a linker between BBS4 and BBS8. We also applied the VIP assay to mapping subunit interactions of the Exocyst tethering complex. In addition, by individually subtracting the eight Exocyst subunits from multisubunit interaction assays, we unequivocally demonstrated one-to-many subunit interactions (Exo70 with Sec10+Sec15, and Exo84 with Sec10+Sec15+Exo70). The simple, versatile VIP assay described here will pave the way to understanding the architectures and functions of multisubunit complexes involved in a variety of cellular processes. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.168740
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    ABSTRACT: Synaptotagmin 1 (Syt1) is a synaptic vesicle protein important for the kinetics of both exocytosis and endocytosis, and is thus a candidate molecule to link these two processes. While the tandem calcium-binding C2 domains of Syt1 have important roles in exocytosis and endocytosis, the function of the conserved juxtamembrane (jxm) linker region has yet to be determined. We now demonstrate that the jxm region of Syt1 interacts directly with the pleckstrin homology (PH) domain of the endocytic protein dynamin 1. Using millisecond time resolution, cell-attached capacitance recordings to monitor clathrin-mediated endocytosis of single vesicles in neuroendocrine chromaffin cells, we find that loss of this interaction prolongs the duration of the fission pore leading to defects in the dynamics of vesicle fission. These results indicate a previously undescribed interaction between two major regulatory proteins in the secretory vesicle cycle and that this interaction regulates endocytosis. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.161505
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    ABSTRACT: The contractile vacuole complex (CVC) of Trypanosoma cruzi, the etiologic agent of Chagas disease, collects and expels excess water as a mechanism of regulatory volume decrease after hyposmotic stress and has also a role in cell shrinking after hyperosmotic stress. Here we report that, in addition to its role in osmoregulation, the CVC of T. cruzi has a role in the biogenesis of acidocalcisomes. Expression of dominant negative mutants of the CVC-located small GTPase Rab32 results in lower numbers of less electron-dense acidocalcisomes, lower content of polyphosphate, lower capacity for acidocalcisome acidification and Ca(2+) uptake driven by the vacuolar proton pyrophosphatase and the Ca(2+)-ATPase, respectively, and less infective parasites, revealing the role of this organelle in parasite infectivity. We also provide further fluorescence, electron microscopy and electron tomography evidence of the active contact of acidocalcisomes with the CVC, suggesting an active exchange of proteins between the two organelles. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.169466
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    ABSTRACT: Autocrine VEGF is necessary for endothelial survival, although the cellular mechanisms supporting this function are unknown. Here we show that even after full differentiation and maturation, continuous expression of VEGF by endothelial cells is needed to sustain vascular integrity and cellular viability. Depletion of VEGF from the endothelium results in mitochondria fragmentation and suppression of glucose metabolism leading to increased autophagy that contributes to cell death. Gene expression profiling showed that endothelial VEGF contributes to the regulation of cell cycle and mitochondrial gene clusters, as well as several, but not all, targets of the transcription factor FOXO1. Indeed, VEGF-deficient endothelium in vitro and in vivo showed increased levels of FOXO1 protein in the nucleus and cytoplasm. Silencing of FOXO1 in VEGF-depleted cells reversed expression profiles of several of the gene clusters that were de-regulated in VEGF knockdown, and rescued both cell death and autophagy phenotypes. Our data suggest that endothelial VEGF maintains vascular homeostasis through regulation of FOXO1 levels thereby ensuring physiological metabolism and endothelial cell survival. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 05/2015; DOI:10.1242/jcs.163774