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: The minimal machinery mediating store operated Ca(2+) entry (SOCE) include an ER Ca(2+) sensor -STIM1- and a plasma membrane (PM) Ca(2+)-selective channel Orai1. Here we quantitatively dissect Orai1 trafficking dynamics and show that Orai1 recycles rapidly at the PM (Kex ≃ 0.1 min(-1)), with ∼40% of the total Orai1 pool localizing to the PM at steady state. A subset of intracellular Orai1 localizes to a sub-plasmalemal compartment. Store depletion is coupled to Orai1 PM enrichment in a STIM1-dependent fashion. This is due to trapping of Orai1 into cortical ER STIM1 clusters leading to its removal from the recycling pool and enrichment at the PM. Interestingly at high STIM1 expression Orai1 is trapped into STIM1 clusters intracellularly, thus preventing its PM enrichment following store depletion. Consistently, STIM1 knockdown prevents trapping of excess Orai1 into limiting STIM1 clusters in the cortical ER. SOCE-dependent Ca(2+) influx shows a similar biphasic dependence on the Orai1:STIM1 ratio. Therefore, a STIM1-dependent Orai1 "trafficking trap" mechanism controls Orai1 PM enrichment and SOCE levels, thus modulating SOCE bandwidth for downstream signaling. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.172320
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    ABSTRACT: Alternative splicing (AS) is one of the major mechanisms to warrant the proteomic and functional diversity of eukaryotes. However, the complex nature of the splicing machinery, its associated splicing regulators and the functional implications of alternatively spliced transcripts is only poorly understood.We investigated here the functional role of the splicing regulator rbfox1 in vivo using the zebrafish as a model system. We find that loss-of rbfox1 leads to progressive cardiac contractile dysfunction and heart failure. By using deep-transcriptome sequencing and quantitative real-time PCR we show that depletion of rbfox1 in zebrafish results in an altered isoform expression of several crucial target genes, such as actn3a and hug.This study underlines that tightly regulated splicing is necessary for unconstrained cardiac function and renders the splicing regulator rbfox1 an interesting target to be investigated in human heart failure and cardiomyopathy. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.166850
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    ABSTRACT: Human airway basal cells (BC) are the stem/progenitor population of the airway epithelium, and play a central role in anchoring the epithelium to the basement membrane. The anatomic position of BC allows for potential paracrine signaling between BC and the underlying non-epithelial stromal cells. In support of this, we previously demonstrated endothelial cells (EC) support growth of BC during co-culture via vascular endothelial growth factor A (VEGFA)-mediated signaling. Building on these findings, RNA sequencing analysis demonstrated that BC express multiple fibroblast growth factor (FGF) ligands (FGF2, 5, 11 and 13) with only FGF2 and FGF5 capable of functioning in a paracrine manner to activate classical FGF receptor (FGFR) signaling. Antibody mediated blocking of FGFR1 during BC-EC co-culture significantly reduced EC dependent BC growth. Stimulation of EC via BC-derived growth factors resulted in EC expression of matrix metallopeptidase 14 (MMP14) and shRNA mediated knockdown of EC MMP14 significantly reduced EC dependent growth of BC. Overall, these data characterize a novel growth factor mediated reciprocal "cross-talk" between human airway BC and EC that regulates proliferation of BC. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.168179
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    ABSTRACT: In the nervous system, attractive and repulsive factors guide neuronal growth, pathfinding and target innervation during development, learning and regeneration after injury. Repulsive and growth-inhibitory factors, such as some ephrins, semaphorins, netrins and myelin-associated growth inhibitors, restrict nerve fiber growth, whereas neurotrophins, and other ephrins, semaphorins and netrins attract fibers and promote neurite growth. Several of these guidance molecules also play crucial roles in vasculogenesis, and regulate cell migration and tissue formation in different organs. Precise and highly specific signal transduction in space and time is required in all these cases, which primarily depends on the presence and function of specific receptors. Interestingly, many of these ligands act through multi-subunit receptor complexes. In this Commentary, we review the current knowledge of how complexes of the receptors for attractive and repulsive neurite growth regulatory factors are reorganized in a spatial and temporal manner, and reveal the implications that such dynamics have on the signaling events that coordinate neurite fiber growth. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.165555
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    ABSTRACT: Acute lung injury (ALI) during sepsis is characterized by bilateral alveolar infiltrates, lung edema, and respiratory failure. Here, we examined the efficacy of DNA methyl transferase (DNMT) inhibitor Aza (5-Aza 2-deoxycytidine), histone deacetylase (HDAC) inhibitor TSA (Trichostatin A), and combination therapy (Aza+TSA) in protection of ALI. In LPS-induced mouse ALI, post-treatment with a single dose of Aza+TSA showed a substantial attenuation of adverse lung histopathological changes, and inflammations. Importantly, these protective effects were due to significant macrophage phenotypic changes observed in LPS-stimulated macrophages treated with Aza+TSA as compared with untreated LPS-induced macrophages or LPS-stimulated macrophages treated with either drug alone. Further, we observed significantly lower levels of pro-inflammatory molecules and higher levels of anti-inflammatory molecules in LPS-induced macrophages treated with Aza+TSA than in LPS-induced macrophages treated with either drug alone. The protection was ascribed to dual effects by an inhibition of MAPK-HuR-TNF and activation of STAT3-Bcl2 pathways. Combinatorial treatment with Aza+TSA reduces inflammation and promotes an anti-inflammatory M2 macrophage phenotype in ALI. This finding gives further evidence that the epigenetic treatment has a therapeutic potential for patients with sepsis. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.170258
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    ABSTRACT: Paxillin (PXN) is a focal adhesion protein implicated in signal transduction from the extracellular matrix. Recently, it has been shown to shuttle between the cytoplasm and the nucleus. When inside the nucleus, paxillin promotes cell proliferation. Here, we introduce paxillin as a transcriptional regulator of IGF2 and H19 genes. It does not affect the allelic expression of the two genes; rather, it regulates long-range chromosomal interactions between IGF2 or H19 promoter and a shared distal enhacer on an active allele. Specifically, paxillin stimulates the interaction between the enhancer and the IGF2 promoter, thus activating IGF2 gene transcription, while it restrains the interaction between the enhancer and the H19 promoter, downregulating the H19 gene. We found that paxillin interacts with cohesin and Mediator which have been shown to mediate long-range chromosomal looping. We propose that these interactions occur at the IGF2/H19 gene cluster and are involved in the formation of loops between the IGF2/H19 promoters and the enhacer, and thus the expression of corresponding genes. These observations contribute to a mechanistic explanation of paxillin's role in proliferation and fetal development. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.170985
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    ABSTRACT: Endothelial cell-cell junctions maintain a restrictive barrier that is tightly regulated to allow dynamic responses to permeability-inducing angiogenic factors as well as inflammatory agents and adherent leukocytes. The ability of these stimuli to transiently remodel adherens junctions (AJs) depends on Rho-GTPase-controlled cytoskeletal rearrangements. How activity of Rho-GTPases is spatio-temporally controlled at endothelial AJs by guanine-nucleotide exchange factors (GEFs) is incompletely understood. Here, we identify a crucial role for the Rho-GEF Trio in stabilizing VE-cadherin-based junctions. Trio interacts with VE-cadherin and locally activates Rac1 at AJs during nascent contact formation, assessed using a novel FRET-based Rac1 biosensor and biochemical assays. The Rac-GEF domain of Trio is responsible for remodeling of junctional actin from radial to cortical actin bundles, a critical step for junction stabilization. This promotes the formation of linear AJs and increases endothelial monolayer resistance. Collectively, our data show the importance of spatio-temporal regulation of the actin cytoskeleton through Trio and Rac1 at VE-cadherin-based cell-cell junctions to maintain the endothelial barrier. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.168674
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    ABSTRACT: Mesenchymal stem cells (MSCs) are among the most promising and suitable stem cell types for vascular tissue engineering. Substantial effort has been made to differentiate MSCs towards vascular cell phenotypes, including endothelial cells and smooth muscle cells (SMCs). The microenvironment of vascular cells not only contains biochemical factors that influence differentiation, but also exerts hemodynamic forces, such as shear stress and cyclic strain. Recent evidence has shown that these forces can influence the differentiation of MSCs into endothelial cells or SMCs. In this Commentary, we present the main findings in the area with the aim of summarizing the mechanisms by which shear stress and cyclic strain induce MSC differentiation. We will also discuss the interactions between these mechanical cues and other components of the microenvironment, and highlight how these insights could be used to maintain differentiation. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.167783
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    ABSTRACT: Reactive oxygen species (ROS) produced by the NADPH oxidase (NOX) complex play important physiological and pathological roles in neurotransmission and neurodegeneration, respectively. However, the contribution of ROS to molecular mechanisms involved in neuronal polarity and axon elongation is not well understood. In this work, we found that loss of function of the NOX complex altered neuronal polarization and decreased axonal length by a mechanism that involves actin cytoskeleton dynamics. Together, these results indicate that physiological levels of ROS produced by the NOX complex modulate hippocampal neuronal polarity and axonal growth in vitro. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.168567
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    ABSTRACT: The neural cell adhesion molecule (NCAM) is important during neural development, because it contributes to neurite outgrowth in response to its ligands at the cell surface. In the adult brain NCAM is involved in regulating synaptic plasticity. The molecular mechanisms underlying delivery of NCAM to the neuronal cell surface remain poorly understood. We used a protein macroarray and identified the kinesin light chain 1 (KLC1), a component of the kinesin-1 motor protein, as a binding partner of the intracellular domains of the two transmembrane isoforms of NCAM, NCAM140 and NCAM180. KLC1 binds to amino acids CGKAGPGA within the intracellular domain of NCAM and co-localizes with kinesin-1 in the Golgi compartment. Delivery of NCAM180 to the cell surface is increased in CHO cells and neurons co-transfected with kinesin-1. We further demonstrate that the p21-activated kinase 1 (PAK1) competes with KLC1 for binding to the intracellular domain of NCAM and contributes to the regulation of the membrane insertion of NCAM. Our results indicate that NCAM is delivered to the cell surface via a kinesin-1 mediated transport mechanism in a PAK1-dependent manner. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.169391
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    ABSTRACT: The breaching of cellular and structural barriers by migrating cells is a driving factor in development, inflammation and tumor cell metastasis. One of the most extensively studied examples is the extravasation of activated leukocytes across the vascular endothelium, the inner lining of blood vessels. Each step of this leukocyte transendothelial migration (TEM) process is regulated by distinct endothelial adhesion receptors such as the intercellular adhesion molecule 1 (ICAM1). Adherent leukocytes exert force on these receptors, which sense mechanical cues and transform them into localized mechanosignaling in endothelial cells. In turn, the function of the mechanoreceptors is controlled by the stiffness of the endothelial cells and of the underlying substrate representing a positive-feedback loop. In this Commentary, we focus on the mechanotransduction in leukocytes and endothelial cells, which is induced in response to variations in substrate stiffness. Recent studies have described the first key proteins involved in these mechanosensitive events, allowing us to identify common regulatory mechanisms in both cell types. Finally, we discuss how endothelial cell stiffness controls the individual steps in the leukocyte TEM process. We identify endothelial cell stiffness as an important component, in addition to locally presented chemokines and adhesion receptors, which guides leukocytes to sites that permit TEM. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.163055
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    ABSTRACT: Retrograde trafficking from the Golgi apparatus to endoplasmic reticulum (ER) via COPI-coated vesicles has been implicated in lipid homeostasis. Here we found that a block in COPI-dependent retrograde trafficking promoted processing and nuclear translocation of SREBPs (sterol regulatory element binding proteins) and upregulated expression of downstream genes involved in lipid biosynthesis. This elevation in SREBP processing/activation was not caused by mislocalization of S1P or S2P, two Golgi-resident endoproteases involved in SREBP processing, but instead by increased Golgi residence of SREBPs, leading to their increased susceptibility to processing by the endoproteases. Analyses using a processing-defective SREBP mutant suggested that a fraction of SREBP molecules undergo basal cycling between the ER and Golgi in complex with SCAP (SREBP cleavage-activating protein). Furthermore, we showed that SCAP alone is retrieved back from the Golgi to the ER after processing of SREBP under sterol-deficient conditions. Thus, our observations indicate that COPI-mediated retrograde trafficking is critical for preventing unnecessary SREBP activation through retrieval of the SCAP-SREBP complex that basally escapes from the sterol-regulated ER retention machinery, as well as for reuse of SCAP. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.164137
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    ABSTRACT: Protein kinase A (PKA) accumulates at the base of the cilium where it negatively regulates the Hedgehog (Hh) pathway. Although PKA activity is essentially controlled by the cAMP produced by Adenylyl Cyclases (AC), the influence of these enzymes on the Hh pathway remains unclear. Here we show that AC5 and AC6 are the two isoforms most strongly expressed in cerebellar granular neuron precursors (CGNPs) and that that while over-expression of AC5 and AC6 represses the Hh pathway, their knockdown results in the activation of this pathway in CGNPs and in the embryonic neural tube (NT). Indeed, AC5 and AC6 concentrate in the primary cilium, and mutation of a previously undescribed cilium targeting motif in AC5 suppresses its ciliary location, as well as its capacity to inhibit Hh signalling. Stimulatory and inhibitory Gα proteins, that are engaged by the G protein coupled receptors (GPCRs), control AC5 and AC6 activity and regulate Hh pathway in CGNPs and NT. Therefore, we propose that the activity of different ciliary GPCRs converge on AC5 and AC6 to control PKA activity and hence the Hh pathway. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.172635
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    ABSTRACT: PACSIN2, a membrane-sculpting BAR domain protein, localizes to caveolae. Here, we found that PKC phosphorylates PACSIN2 at serine 313, thereby decreasing its membrane binding and tubulation capacities. Concomitantly, phosphorylation decreased the time span for which caveolae could be tracked at the plasma membrane (the 'tracking-duration'). Analyses of the phospho-mimetic S313E mutant suggested that PACSIN2 phosphorylation is sufficient to reduce caveolar tracking-durations. Both hypotonic treatment and isotonic drug-induced PKC activation increased PACSIN2 phosphorylation at serine 313 and shortened caveolar tracking-durations. Caveolar tracking-durations were also reduced upon the expression of other membrane-binding deficient PACSIN2 mutants or RNAi-mediated PACSIN2 depletion, pointing to a role of PACSIN2 levels for the lifetime of caveolae. Interestingly, the decrease in membrane-bound PACSIN2 was inversely correlated with the recruitment and activity of dynamin 2, a GTPase mediating membrane scission. Furthermore, expression of EHD2, which stabilizes caveolae and binds to PACSIN2, restored the tracking-durations of cells with reduced PACSIN2 levels. These findings suggest that the PACSIN2 phosphorylation decreases its membrane-binding activity, thereby decreasing its stabilizing effect on caveolae and triggering dynamin-mediated removal of caveolae. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.167775
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    ABSTRACT: Endocytosis is an essential cellular process that is often hijacked by pathogens and pathogenic products. Endocytic processes can be classified into two broad categories, dependent or not on clathrin. The SNARE proteins VAMP2, 3 and 8 are internalized in a clathrin-dependent manner. Yet, the full scope of their endocytic behavior has not yet been elucidated. Here, we found that VAMP2, 3, and 8 are localized on plasma membrane invaginations and very early uptake structures that are induced by the bacterial Shiga toxin, which enters cells by clathrin-independent endocytosis. We show that toxin trafficking into cells and cell intoxication rely on these SNARE proteins. Of note, the cellular uptake of VAMP2, 3, and 8 is increased in the presence of Shiga toxin, even when their clathrin-dependent endocytosis is blocked. We therefore conclude that VAMP2, 3, and 8 are removed from the plasma membrane via non-clathrin pathways, in addition to their clathrin-dependent uptake. Moreover, our study identifies these SNARE proteins as the first transmembrane trafficking factors that functionally associate at the plasma membrane with the toxin-driven clathrin-independent uptake process. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.171116
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    ABSTRACT: Cell growth and division are tightly coordinated to maintain cell size constant during successive cell cycles. In S.pombe the SAD kinase Cdr2 regulates cell size at division and division plane positioning. Cdr2 forms nodes on the medial cortex containing an inhibitory pathway for Wee1, under the negative control of polar gradients of the DYRK kinase Pom1. This pathway involves the SAD kinase Cdr1, a direct inhibitor of Wee1. Cdr2 also interacts with the anillin Mid1 which defines the division plane, and with additional components of medial cortical node, including Blt1, which participate in their mitotic promoting and cytokinetic functions. We show that Cdr2 interaction with Wee1 and Mid1 requires Cdr2 UBA domain necessary for its kinase activity. In contrast, Cdr1 associates with Cdr2 C-terminus composed of basic and KA-1 lipid-binding domains. Mid1 also interacts with Cdr2 C-terminus and may bridge the N- and C-terminal domains while Blt1 associates with the central spacer region. We propose that the association of Cdr2 effectors with different domains may constrain Cdr1 and Wee1 spatially to promote Wee1 inhibition upon Cdr2 kinase activation. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.173146
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    ABSTRACT: Gp78, an ERAD-associated E3 ubiquitin ligase, localizes to mitochondria-associated ER and targets the mitofusin (Mfn1/Mfn2) mitochondrial fusion proteins for degradation. Gp78 is also the cell surface receptor for autocrine motility factor (AMF) that prevents Gp78-dependent mitofusin degradation. Gp78 ubiquitin ligase activity promotes ER-mitochondria association and ER-mitochondria calcium coupling, processes that are reversed by AMF. Electron microscopy of HT-1080 fibrosarcoma cancer cells identified both smooth (∼8 nm) and wider (∼50-60 nm) rough ER-mitochondria contacts. Gp78 shRNA knockdown and AMF treatment selectively reduced the extent of rough ER-mitochondria contacts without impacting smooth ER-mitochondria contacts. Concomitant siRNA knockdown of Mfn1 increased smooth ER-mitochondria contacts in both control and shGp78 cells while knockdown of Mfn2 increased rough ER-mitochondria contacts selectively in shGp78 HT-1080 cells. The mitofusins therefore inhibit ER-mitochondria interaction. Regulation of close ER-mitochondria contacts by Mfn1 and of rough ER-mitochondria contacts by AMF-sensitive Gp78 degradation of Mfn2 define novel mechanisms that regulate ER-mitochondria interactions. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.171132
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    ABSTRACT: A better understanding of molecular regulation in adipogenesis may help develop efficient strategies to cope with obesity-related diseases. Here, we report CCAAT/enhancer binding protein (C/EBP) β and δ, two critical pro-adipogenic transcription factors, are controlled at a translational level by serine/threonine kinase 40 (Stk40). Genetic knockout (KO) or knockdown (KD) of Stk40 leads to increased protein levels of C/EBP proteins and adipocyte differentiation in mouse embryonic fibroblasts (MEFs), fetal liver stromal cells, and mesenchymal stem cells (MSCs). In contrast, overexpression of Stk40 abolishes the enhanced C/EBP protein translation and adipogenesis observed in Stk40-KO/KD cells. Functionally, knockdown of C/EBPβ eliminates the enhanced adipogenic differentiation in Stk40-KO/KD cells substantially. Mechanistically, deletion of Stk40 enhances phosphorylation of eIF4E-binding protein 1, leading to increased eIF4E-dependent translation of C/EBPβ and C/EBPδ. Knockdown of eIF4E in MSCs decreases translation of C/EBP proteins. Moreover, Stk40-KO fetal livers display an increased adipogenic program and aberrant lipid/steroid metabolism. Collectively, our study uncovers a new repressor of C/EBP protein translation as well as adipogenesis and provides new insights into the molecular mechanism underpinning the adipogenic program. © 2015. Published by The Company of Biologists Ltd.
    Journal of Cell Science 06/2015; DOI:10.1242/jcs.170282