Molecular Biology of the Cell (MOL BIOL CELL )

Publisher: American Society for Cell Biology, American Society for Cell Biology


Molecular Biology of the Cell, the journal owned and published by The American Society for Cell Biology, publishes papers that describe and interpret results of original research concerning the molecular aspects of cell structure and function. Studies whose scope bridges several areas of biology are particularly encouraged, for example cell biology and genetics. The aim of the Journal is to publish papers describing substantial research progress in full: papers should include all previously unpublished data and methods essential to support the conclusions drawn.

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  • Website
    Molecular Biology of the Cell website
  • Other titles
    Molecular biology of the cell, MBC
  • ISSN
  • OCLC
  • Material type
    Periodical, Internet resource
  • Document type
    Journal / Magazine / Newspaper, Internet Resource

Publisher details

American Society for Cell Biology

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • On authors personal web site or institutional digital archives
    • Publisher's version/PDF must be used
    • Publisher copyright and source must be acknowledged
    • Must link to publisher version
    • Articles are placed in PubMed Central after 2 months
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: When Dictyostelium cells are hyper-osmotically stressed STATc is activated by tyrosine phosphorylation. Unusually, activation is regulated by serine phosphorylation and consequent inhibition of a tyrosine phosphatase: PTP3. The identity of the cognate tyrosine kinase is unknown and we show that two Tyrosine Kinase-Like (TKL) enzymes, Pyk2 and Pyk3, share this function; thus for stress-induced STATc activation, single null mutants are only marginally impaired but the double mutant is non-activatable. When cells are stressed Pyk2 and Pyk3 undergo increased auto-catalytic tyrosine phosphorylation. The site(s) that are generated bind the SH2 domain of STATc and then STATc becomes the target of further kinase action. The signaling pathways that activate Pyk2 and Pyk3 are only partially overlapping and there may be a structural basis for this difference because Pyk3 contains both a TKL domain and a pseudokinase domain. The latter functions, like the JH2 domain of metazoan JAKs, as a negative regulator of the kinase domain. The fact that two differently regulated kinases catalyse the same phosphorylation event may facilitate specific targeting because under stress Pyk3 and Pyk2 accumulate in different parts of the cell; Pyk3 moves from the cytosol to the cortex while Pyk2 accumulates in cytosolic granules that colocalise with PTP3.
    Molecular Biology of the Cell 08/2014;
  • [Show abstract] [Hide abstract]
    ABSTRACT: Following ER Ca(2+) depletion, STIM1 and Orai1 complexes assemble autonomously at ER-plasma membrane (PM) junctions to trigger store-operated Ca(2+) influx. One hypothesis to explain this process is a diffusion trap in which activated STIM1 diffusing in the ER becomes trapped at junctions through interactions with the PM, and STIM1 then traps Orai1 in the PM through binding of its CRAC activation domain. We tested this model by analyzing STIM1 and Orai1 diffusion using single-particle tracking, photoactivation of protein ensembles, and Monte Carlo simulations. In resting cells, STIM1 diffusion is Brownian while Orai1 is slightly subdiffusive. After store depletion both proteins slow to the same speeds, consistent with complex formation, and are confined to a corral similar in size to ER-PM junctions. While the escape probability at high STIM:Orai expression ratios is <1%, it is significantly increased by reducing the affinity of STIM1 for Orai1 or by expressing the two proteins at comparable levels. Our results provide direct evidence that STIM-Orai complexes are trapped by their physical connections across the junctional gap, but also reveal that the complexes are surprisingly dynamic, suggesting that readily reversible binding reactions generate free STIM1 and Orai1 which engage in constant diffusional exchange with extrajunctional pools.
    Molecular Biology of the Cell 07/2014;
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    ABSTRACT: Filopodia are long plasma membrane extensions involved in the formation of adhesive, contractile, and protrusive actin-based structures in spreading and migrating cells. Whether or not filopodia formed by different molecular mechanisms equally support these cellular functions is unresolved. We used Ena/VASP-deficient MV(D7) fibroblasts, which are also devoid of endogenous mDia2, as a model system to investigate how these different actin regulatory proteins impact filopodia morphology and dynamics independently of the other. Filopodia initiated by either Ena/VASP or mDia2 contained similar molecular inventory, but differed significantly in parameters such as number, length, F-actin organization, lifetime, and protrusive persistence. Moreover, in the absence of Ena/VASP, filopodia generated by mDia2 did not support initiation of integrin-dependent signaling cascades required for adhesion and subsequent lamellipodial extension, thereby causing a defect in early cell spreading. Co-expression of VASP with constitutively active mDia2(M/A) rescued these early adhesion defects. We conclude that Ena/VASP and mDia2 support the formation of filopodia with significantly distinct properties, and that Ena/VASP regulates mDia2-initiated filopodial morphology, dynamics, and function.
    Molecular Biology of the Cell 07/2014;
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    ABSTRACT: The biological functions of NFκB1 (p50) have not been studied as often as other members of the NFκB family due to its lack of a transcriptional domain. Our recently studies demonstrate that p50 functions as an apoptotic mediator via its inhibition of GADD45α protein degradation and increase in p53 protein translation. Here, we reported a novel function of p50 in its regulation of SOD2 transcription via the NFκB-independent pathway. We found that the deletion of p50 in MEFs (p50-/-) upregulated SOD2 expression at both protein and mRNA levels. SOD2 promoter-driven luciferase was also upregulated in p50-/- cells compared with that in wide-type MEF (p50+/+) cells, suggesting p50 regulation of SOD2 at transcriptional level. Our results also showed that p50-deficiency specifically resulted in down-regulation of phosphorylation and an increase transactivation of FoxO3a compared with WT cells. Further studies indicated that p50-down-regulated FoxO3a phosphorylation was mediated by activated Akt via up-regulation of miR-190, in turn inhibiting PHLPP1 translation. Together, our studies identify a p50 novel function in the regulation of SOD2 transcription via modulating of the miR-190/PHLPP1/Akt-FoxO3a pathway, which provides significant insight into understanding of the p50 physiological function.
    Molecular Biology of the Cell 09/2013;
  • Molecular Biology of the Cell 01/2011; 22}, Meeting Abstract = {2288.
  • Molecular Biology of the Cell; 01/2009
  • Molecular Biology of the Cell 01/2009;
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    ABSTRACT: The Rho-type GTPase Cdc42 is a central regulator of eukaryotic cell polarity and signal transduction. In budding yeast, Cdc42 regulates polarity and mitogen-activated protein (MAP) kinase signaling in part through the PAK-family kinase Ste20. Activation of Ste20 requires a Cdc42/Rac interactive binding (CRIB) domain, which mediates its recruitment to membrane-associated Cdc42. Here, we identify a separate domain in Ste20 that interacts directly with membrane phospholipids and is critical for its function. This short region, termed the basic-rich (BR) domain, can target green fluorescent protein to the plasma membrane in vivo and binds PIP(2)-containing liposomes in vitro. Mutation of basic or hydrophobic residues in the BR domain abolishes polarized localization of Ste20 and its function in both MAP kinase-dependent and independent pathways. Thus, Cdc42 binding is required but is insufficient; instead, direct membrane binding by Ste20 is also required. Nevertheless, phospholipid specificity is not essential in vivo, because the BR domain can be replaced with several heterologous lipid-binding domains of varying lipid preferences. We also identify functionally important BR domains in two other yeast Cdc42 effectors, Gic1 and Gic2, suggesting that cooperation between protein-protein and protein-membrane interactions is a prevalent mechanism during Cdc42-regulated signaling and perhaps for other dynamic localization events at the cell cortex.
    Molecular Biology of the Cell 01/2008; 18(12):4945-56.