自引率: 3.8%
被引量: 43204
通过率: 暂无数据
审稿周期: 1.4
版面费用: 暂无数据
国人发稿量: 25
投稿须知/期刊简介:
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).
期刊描述简介:
Journal of Cell Science is an international peer-reviewed journal in the field of cell biology that is published by The Company of Biologists, a not-for-profit charitable organisation run by biologists for the benefit of the biological community. Journal of Cell Science is committed to publishing the full range of topics in cell biology, and the single most important criterion for acceptance is scientific excellence. Articles must therefore pose and test a significant hypothesis that will provide novel perspectives and approaches to understanding cell biology, and will stimulate the interest of the broad readership of the journal (see aims and scope). All research articles published in Journal of Cell Science are subject to rigorous single-blind peer review, and editorial decisions are made by a team of research-active academics in the field, supported by an international Editorial Advisory Board. In addition to primary research articles, Journal of Cell Science publishes a range of commissioned review-based articles aimed at synthesising the latest advances in the field, putting forward new hypotheses to provoke debate and inspire new research directions, and educating newcomers to the field. For more information on publishing in Journal of Cell Science, please visit our submission, manuscript preparation, article types and journal policies pages. Journal of Cell Science offers advance posting of accepted author manuscripts on its Accepted manuscripts page, which is updated daily. Publication of the final version of record is by a continuous publication model - as soon as an article is ready to be published, it is immediately released online rather than waiting for other articles in the issue to be completed, resulting in faster access to the final version of the article. Journal of Cell Science [ISSN 1477-9137 (online); ISSN 0021-09533 (print)] is a continuation of The Quarterly Journal of Microscopical Science (ISSN 0370-2952).
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Role of CBP in regulating HIF-1-mediated activation of transcription.
The hypoxia-inducible factor-1 (HIF-1) is a key regulator of oxygen homeostasis in the cell. We have previously shown that HIF-1alpha and the transcriptional coactivator CBP colocalize in accumulation foci within the nucleus of hypoxic cells. In our further exploration of the hypoxia-dependent regulation of HIF-1alpha function by transcriptional coactivators we observed that coexpression of SRC-1 (another important coactivator of the hypoxia response) and HIF-1alpha did not change the individual characteristic nuclear distribution patterns. Colocalization of both these proteins proved to be mediated by CBP. Biochemical assays showed that depletion of CBP from cell extracts abrogated interaction between SRC-1 and HIF-1alpha. Thus, in contrast to the current model for the assembly of complexes between nuclear hormone receptors and coactivators, the present data suggest that it is CBP that recruits SRC-1 to HIF-1alpha in hypoxic cells. We also observed that CBP, HIF-1alpha/Arnt and HIF-1alpha/CBP accumulation foci partially overlap with the hyperphosphorylated form of RNA polymerase II, and that CBP had a stabilizing effect on the formation of the complex between HIF-1alpha and its DNA-binding partner, Arnt. In conclusion, CBP plays an important role as a mediator of HIF-1alpha/Arnt/CBP/SRC-1 complex formation, coordinating the temporally and hierarchically regulated intranuclear traffic of HIF-1alpha and associated cofactors in signal transduction in hypoxic cells.
被引量：46 发表：1970
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Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism.
The transcriptional regulation of several dozen genes in response to low oxygen tension is mediated by hypoxia-inducible factor 1 (HIF-1), a heterodimeric protein composed of two subunits, HIF-1alpha and HIF-1beta. In the HIF-1alpha-deficient human leukemic cell line, Z-33, exposed to mild (8% O(2)) or severe (1% O(2)) hypoxia, we found significant upregulation of two related heterogenous nuclear ribonucleoproteins, RNA-binding motif protein 3 (RBM3) and cold inducible RNA-binding protein (CIRP), which are highly conserved cold stress proteins with RNA-binding properties. Hypoxia also induced upregulation of RBM3 and CIRP in the murine HIF-1beta-deficient cell line, Hepa-1 c4. In various HIF-1 competent cells, RBM3 and CIRP were induced by moderate hypothermia (32 degrees C) but hypothermia was ineffective in increasing HIF-1alpha or vascular endothelial growth factor (VEGF), a known HIF-1 target. In contrast, iron chelators induced VEGF but not RBM3 or CIRP. The RBM3 and CIRP mRNA increase after hypoxia was inhibited by actinomycin-D, and in vitro nuclear run-on assays demonstrated specific increases in RBM3 and CIRP mRNA after hypoxia, which suggests that regulation takes place at the level of gene transcription. Hypoxia-induced RBM3 or CIRP transcription was inhibited by the respiratory chain inhibitors NaN(3) and cyanide in a dose-dependent fashion. However, cells depleted of mitochondria were still able to upregulate RBM3 and CIRP in response to hypoxia. Thus, RBM3 and CIRP are adaptatively expressed in response to hypoxia by a mechanism that involves neither HIF-1 nor mitochondria.
被引量：119 发表：1970
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Anaphase onset does not require the microtubule-dependent depletion of kinetochore and centromere-binding proteins.
Spindle checkpoint proteins, such as Mad2 and BubR1, and the motors dynein/dynactin and CENP-E usually leave kinetochores prior to anaphase onset by microtubule-dependent mechanisms. Likewise, 'chromosome passenger proteins' including INCENP are depleted from the centromeres after anaphase onset and then move to the midzone complex, an event that is essential for cytokinesis. Here we test whether the cell cycle changes that occur at anaphase onset require or contribute to the depletion of kinetochore and centromere proteins independent of microtubules. This required the development of a novel non-antibody method to induce precocious anaphase onset in vivo by using a bacterially expressed fragment of the spindle checkpoint protein Mad1 capable of activating the APC/C, called GST-Mad1F10. By injecting PtK1 cells in nocodazole with GST-Mad1F10 and processing the cells for immunofluorescence microscopy after anaphase sister chromatid separation in nocodazole we found that Mad2, BubR1, cytoplasmic dynein, CENP-E and the 3F3/2 phosphoepitope remain on kinetochores. Thus depletion of these proteins (or phosphoepitope) at kinetochores is not required for anaphase onset and anaphase onset does not produce their depletion independent of microtubules. In contrast, both microtubules and anaphase onset are required for depletion of the 'chromosome passenger' protein INCENP from centromeres, as INCENP does not leave the chromosomes prior to anaphase onset in the presence or absence of microtubules, but does leave the centromeres after anaphase onset in the presence of microtubules.
被引量：13 发表：2002
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Involvement of CD44 in cytoskeleton rearrangement and raft reorganization in T cells.
:T cell activation is accompanied by actin-mediated receptor clustering and reorganization of lipid rafts. It has been suggested that costimulatory molecules might be involved in these processes. We here provide evidence that engagement of the adhesion molecule CD44 initiates cytoskeletal rearrangement and membrane reorganization in T cells. Cross-linking of CD44 on a T helper line was accompanied by adhesion, spreading and actin bundle formation. These processes were energy dependent and required an intact actin and microtubule system. They involved the small GTPase Rac as evidenced by the absence of spreading in cells overexpressing a dominant negative form of Rac. The CD44 initiated reorganization of the cytoskeleton was associated with the recruitment of CD44 and the associated tyrosine phosphokinases p56(lck) and p59(fyn) into glycolipid enriched membrane microdomains (GEM). We interpret the data in the sense that CD44 functions as a costimulatory molecule in T cell activation by inducing actin cytoskeletal rearrangements and membrane protein and lipid reorganization including its association with GEMs. Due to the association of CD44 with lck and fyn this colocalization with the TCR allows an abundant provision of these kinases, which are essential to initiate the TCR signaling cascade.
被引量：35 发表：2001
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Illuminating the secretory pathway: when do we need vesicles?
:Recent studies using GFP-tagged markers and time-lapse microscopy have allowed direct visualisation of membrane traffic in the secretory pathway in living mammalian cells. This work shows that larger membrane structures, 300-500 nm in size, are the vehicles responsible for long distance, microtubule-dependent ER-to-Golgi and trans-Golgi to plasma membrane transport of secretory markers. At least two retrograde transport pathways from the Golgi to the ER exist, both of which are proposed to involve a further class of long, tubular membrane carrier that forms from the Golgi and fuses with the ER. Together, this has challenged established transport models, raising the question of whether larger pleiomorphic structures, rather than small 60-80 nm transport vesicles, mediate long-range transport between the ER and Golgi and between the Golgi and plasma membrane.
被引量：- 发表：2001
