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: 5.43

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 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 dynamic assembly and disassembly of actin filaments is essential for the formation and transport of vesicles during endocytosis. In yeast, two types of actin structures, namely cortical patches and cytoplasmic cables, play a direct role in endocytosis, but how their interaction is regulated remains unclear. Here we show that Srv2/CAP, an evolutionally conserved actin regulator, is required for efficient endocytosis due to its role in the formation of the actin patches that aid in initial vesicle invagination and the actin cables that these move along. Deletion of the SRV2 gene results in the appearance of aberrant fragmented actin cables that frequently moved past actin patches, the sites of endocytosis. We find that the C-terminal CARP domain of Srv2p is vitally important for the proper assembly of actin patches and cables; we also demonstrate that Srv2's N terminal HFD domain is required for its localization to actin patches, specifically to the ADP-actin rich region through an interaction with cofilin. These results demonstrate the in vivo roles of Srv2p in the regulation of the actin cytoskeleton during clathrin-mediated endocytosis.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.176651
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    ABSTRACT: Plasma membrane proteins synthesised at the endoplasmic reticulum are delivered to cell surface via sorting pathways. Hydrophobic mismatch theory based on the length of transmembrane domain (TMD) dominates discussion about determinants required for protein sorting to the plasma membrane. Transmembrane adaptor proteins (TRAP) are involved in signalling events taking place at the plasma membrane. Members of this protein family have TMD of varying length. We were interested whether palmitoylation or other motifs contribute to the effective sorting of TRAP proteins. We found that palmitoylation is essential for some but not all TRAP proteins independent of their TMD length. We also provide evidence that palmitoylation and proximal sequences can modulate sorting of artificial proteins with TMD of suboptimal length. Our observations point to a unique character of each TMD defined by its primary amino acid sequence and its impact on membrane protein localisation. We conclude that, in addition to the TMD length, secondary sorting determinants such as palmitoylation or flanking sequences have evolved for the localisation of membrane proteins.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.175190
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    ABSTRACT: Coordination between different cytoskeletal systems is crucial for many cell biological functions, including cell migration and mitosis, and also plays an important role during tissue morphogenesis. Proteins of the class of cytoskeletal crosslinkers or cytolinkers have the ability to interact with more than one cytoskeletal system at a time and are prime candidates to mediate any coordination. One such class comprises the Gas2-like proteins, combining a conserved Calponin-homology-type actin-binding domain and a Gas2 domain predicted to bind microtubules (MTs). This domain combination is also found in spectraplakins, huge cytolinkers that play important roles in many tissues in both invertebrates and vertebrates. Here we dissect the ability of the single Drosophila Gas2-like protein Pigs to interact with both actin and MT cytoskeletons, both in vitro and in vivo, and illustrate complex regulatory interactions that determine Pigs' localisation to and its effects on the cytoskeleton.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.176230
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    ABSTRACT: Some apoptotic processes, such as phosphatidylserine exposure, are potentially reversible without causing cell death. However, phosphatidylserine exposure can induce phagocytosis of a cell, resulting in cell death by phagocytosis: phagoptosis. Phagoptosis of neurons by microglia may contribute to neuropathology, whilst phagoptosis of tumour cells by macrophages may limit cancer. We examined the mechanisms by which BV-2 microglia killed co-cultured pheochromocytoma (PC12) cells, when undifferentiated or differentiated into neuronal cells. We found that microglia activated by lipopolysaccharide rapidly phagocytosed PC12 cells. Activated microglia caused reversible phosphatidylserine exposure on and reversible caspase activation in PC12 cells, and caspase inhibition prevented phosphatidylserine exposure and decreased subsequent phagocytosis. Nitric oxide was necessary and sufficient to induce the reversible phosphatidylserine exposure and phagocytosis. The PC12 cells phagocytosed were not dead and inhibition of their phagocytosis left viable cells. Cell loss was inhibited by blocking phagocytosis at phosphatidylserine, MFG-E8, vitronectin receptors or P2Y6 receptors. Thus activated microglia can induce reversible apoptosis of target cells, which may be insufficient to cause apoptotic cell death, but sufficient to induce their phagocytosis and therefore cell death by phagoptosis.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.174631
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    ABSTRACT: Adapter protein CD2AP (CD2-associated protein) functions in various signaling and vesicle trafficking pathways, including endosomal sorting and/or trafficking and degradation pathways. Here we investigated the role of CD2AP in insulin-dependent glucose transporter 4 (Glut4) trafficking and glucose uptake. Glucose uptake was attenuated in CD2AP-/- podocytes compared with wild-type podocytes in the basal state, and CD2AP-/- podocytes failed to increase glucose uptake in response to insulin. Live cell imaging revealed dynamic trafficking of HA-Glut4-GFP in wild-type podocytes, whereas in CD2AP-/- podocytes HA-Glut4-GFP clustered perinuclearly. In subcellular membrane fractionations, CD2AP co-fractionated with Glut4, IRAP and sortilin, constituents of Glut4 storage vesicles (GSVs). We further found that CD2AP forms a complex with GGA2, a clathrin adaptor, which sorts Glut4 to GSVs, suggesting a role for CD2AP in this process. We also found that CD2AP forms a complex with clathrin and connects clathrin to actin in the perinuclear region. Furthermore, clathrin recycling back to trans-Golgi membranes from the vesicular fraction containing GSVs was defective in the absence of CD2AP. This leads to reduced insulin-stimulated trafficking of GSVs and attenuated glucose uptake into CD2AP-/- podocytes.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.175075
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    ABSTRACT: Regulated mRNA translation is vital for germ cells to produce new proteins in the spatial and temporal patterns that drive gamete development. Translational control involves the de-repression of stored mRNAs and their recruitment by initiation factors (eIF's) to ribosomes. C. elegans expresses five eIF4Es (IFE-1-5); several were shown to selectively recruit unique pools of mRNA. Individual IFE knockouts yield unique phenotypes due to inefficient translation of certain mRNAs. We identified mRNAs preferentially translated via a germline-specific eIF4E isoform, IFE-1. Differential polysome microarray analysis identified 77 mRNAs recruited by IFE-1. Among the IFE-1-dependent mRNAs are several required for late germ cell differentiation and maturation. Polysome association of gld-1, vab-1, vpr-1, rab-7, and rnp-3 mRNAs relies on IFE-1. Live animal imaging showed IFE-1-dependent selectivity in spatial and temporal translation of germline mRNAs. Altered MAPK activation in oocytes suggests dual roles for IFE-1, both promoting and suppressing oocyte maturation at different stages. This single eIF4E isoform exerts positive, selective translational control during germ cell differentiation.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.172684
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    ABSTRACT: Wnt/Wingless (Wg) and Ras/MAPK signaling both play fundamental roles in growth, cell-fate determination, and when dysregulated, can lead to tumorigenesis. Several conflicting modes of interaction between Ras/MAPK and Wnt signaling have been identified in specific cellular contexts, causing synergistic or antagonistic effects on target genes. We find novel evidence that the dual specificity kinase MEK, Downstream of Raf1 (Dsor1), is required for Wnt signaling. Knockdown of Dsor1 results in loss of Wg target gene expression, as well as reductions in stabilized Armadillo (Arm; Drosophila β-catenin). We have identified a close physical interaction between Dsor1 and Arm, and find that catalytically inactive Dsor1 causes a reduction inactive Arm. These results suggest that Dsor1 normally counteracts the Axin-mediated destruction of Arm. We find that Ras-Dsor1 activity is independent of upstream activation by EGFR, rather it appears to be activated by the insulin-like growth factor receptor to promote Wg signaling. Together our results suggest novel crosstalk between Insulin and Wg signaling via Dsor1.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.175240
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    ABSTRACT: Transglutaminases (TG) are externalized from cells via an unknown unconventional secretory pathway. We show for the first time that purinergic signaling regulates active secretion of TG2, an enzyme with a pivotal role in stabilizing extracellular matrices and modulating cell-matrix interactions in tissue repair. Extracellular ATP promotes TG2 secretion by macrophages, and this can be blocked by a purinergic receptor P2X7 (P2X7R)-selective antagonist. Introduction of functional P2X7R into HEK293 cells is sufficient to confer rapid, regulated TG2 export. By employing pharmacological agents, TG2 release could be separated from P2X7R-mediated microvesicle shedding. Neither, Ca2+ signaling alone nor membrane depolarization triggered TG2 secretion which occurred only upon receptor membrane pore formation and without pannexin channel involvement. A gain-of-function mutation in P2X7R associated with autoimmune disease caused enhanced TG2 externalization from cells, and this correlated with increased pore activity. These results provide a mechanistic explanation for a link between active TG2 secretion and inflammatory responses, and aberrant enhanced TG2 activity in certain autoimmune conditions.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.175968
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    ABSTRACT: Maintenance of epithelial polarity depends on the correct localization and levels of polarity determinants. The evolutionarily conserved transmembrane protein Crumbs is crucial for the size and identity of the apical membrane, yet little is known about the molecular mechanisms controlling the amount of Crumbs at the surface. Here, we show that Crumbs levels on the apical membrane depend on a well-balanced state of endocytosis and stabilization. The A: daptor P: rotein 2 (AP-2) complex binds to a motif in the cytoplasmic tail of Crumbs that overlaps with the binding site of Stardust, a protein known to stabilize Crumbs on the surface. Preventing endocytosis by mutations in AP-2 causes expansion of the Crumbs-positive plasma membrane and polarity defects, which can be partially rescued by removing one copy of crumbs. Strikingly, knocking-down both AP-2 and Stardust retains Crumbs on the membrane. This study provides evidence for a molecular mechanism, based on stabilization and endocytosis, to adjust surface levels of Crumbs, which are essential for maintaining epithelial polarity.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.174573
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    ABSTRACT: Our previous research testified that XBP1S is a significant downstream mediator of BMP2 and is involved in BMP2-stimulated chondrocyte differentiation. Herein we report that ATF6 and ATF6a are expressed in growth plate chondrocytes. There are differentially induced during BMP2-triggered chondrocyte differentiation. This differential expression is probably resulted from the activation of the ATF6 gene by Runx2 and repression by Sox6 transcription factor. Runx2 and Sox6 combine with their respective binding elements of ATF6 gene. When overexpressed, ATF6 and ATF6a intensify chondrogenesis; our studies demonstrate that under the stimulation of ATF6 and ATF6a, chondrocytes tend to be hypertrophied and mineralized, a process leading to bone formation. Additionally, lowing expression of ATF6a using its specific siRNA suppresses chondrocyte differentiation. Moreover, ATF6a interacts with Runx2 and augments Runx2-mediated hypertrophied chondrocyte. Importantly, overexpression and knockdown of ATF6a in chondrocyte hypertrophy also lead to altered expressions of IHH and PTHrP. Taken together, these findings indicate that ATF6a favorably controls chondrogenesis and bone formation via a) acting as a co-factor of Runx2 and enhancing Runx2-incited hypertrophic chondrocyte differentiation, and b) affecting IHH/PTHrP signaling.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.169623
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    ABSTRACT: The serotonergic system plays important roles in multiple functions of the nervous system and its malfunctioning leads to neurological and psychiatric disorders. Here, we show that the cell adhesion molecule close homolog of L1 (CHL1), which has been linked to mental disorders, binds to a peptide stretch in the third intracellular loop of the serotonin 2c (5-HT2c) receptor via its intracellular domain. Moreover, we provide evidence that CHL1 deficiency in mice leads to 5-HT2c receptor-related reduction in locomotor activity and reactivity to novelty and that CHL1 regulates signaling pathways triggered by constitutively active isoforms of the 5-HT2c receptor. Furthermore, we found that 5-HT2c receptor and CHL1 co-localize in striatal and hippocampal GABAergic neurons and that 5-HT2c receptor phosphorylation and association of phosphatase and tensin homolog (PTEN) and β-arrestin 2 with the 5-HT2c receptor is regulated by CHL1. Our results demonstrate that CHL1 regulates signal transduction pathways via constitutively active 5-HT2c receptor isoforms, thereby altering 5-HT2c receptor functions and implicating CHL1 as a novel modulator of the serotonergic system.
    Journal of Cell Science 11/2015; DOI:10.1242/jcs.176941
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    ABSTRACT: The scaffold protein Shoc2 accelerates activity of the ERK1/2 pathway. Mutations in Shoc2 result in Noonan-like RASopathy, a developmental disorder with a wide spectrum of symptoms. The amplitude of the ERK1/2 signals transduced through the complex is fine-tuned by the HUWE1-mediated ubiquitination of Shoc2 and its signaling partner RAF-1. Here we provide a mechanistic basis of how ubiquitination of Shoc2 and RAF-1 is controlled. We demonstrate that the newly identified binding partner of Shoc2, the (AAA+) ATPase PSMC5, triggers translocation of Shoc2 to endosomes. At the endosomes PSMC5 displaces the E3-ligase HUWE1 from the scaffolding complex to attenuate ubiquitination of Shoc2 and RAF-1. We show that a Rasopathy mutation that changes the subcellular distribution of Shoc2 leads to alterations in Shoc2 ubiquitination due to the loss of accessibility to PSMC5. In summary, our results demonstrate that PSMC5 is a novel critical player involved in regulating ERK1/2 signal transmission through the remodeling of Shoc2 scaffold complex in a spatially-defined manner.
    Journal of Cell Science 10/2015; DOI:10.1242/jcs.177543