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Molecular Biology of the Cell
Number of Followers: 25  
 
  Partially Free Journal Partially Free Journal
ISSN (Print) 1059-1524 - ISSN (Online) 1939-4586
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  • Bacterial infection and symbiosis

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      Authors: Basler, M; Shao, F.
      Pages: 683 - 684
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0668
      Issue No: Vol. 29, No. 6 (2018)
       
  • Mechanics of cell division and cytokinesis

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      Authors: Canman, J. C; Cabernard, C.
      Pages: 685 - 686
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0671
      Issue No: Vol. 29, No. 6 (2018)
       
  • Ensuring fidelity of chromosome segregation

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      Authors: Unal, E; Torres, J. Z.
      Pages: 687 - 687
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0673
      Issue No: Vol. 29, No. 6 (2018)
       
  • Light, space, and time in cancer signaling

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      Authors: McPherson, P. S; Wu, M.
      Pages: 688 - 688
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0675
      Issue No: Vol. 29, No. 6 (2018)
       
  • The life of a microtubule

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      Authors: Dixit, R; Petry, S.
      Pages: 689 - 689
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0677
      Issue No: Vol. 29, No. 6 (2018)
       
  • Multicellular interactions: regeneration and mechanisms of disease

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      Authors: Niethammer; P.
      Pages: 690 - 690
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0678
      Issue No: Vol. 29, No. 6 (2018)
       
  • Organelles in metabolism and stress responses

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      Authors: Ferguson, S. M; Henne, W. M.
      Pages: 691 - 691
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0679
      Issue No: Vol. 29, No. 6 (2018)
       
  • Organelle morphogenesis, targeting, and distribution

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      Authors: Carlton, J. G; Kornmann, B.
      Pages: 692 - 693
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0681
      Issue No: Vol. 29, No. 6 (2018)
       
  • Lipids and proteins mix it up in Philly

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      Authors: Ma, M; Burd, C. G.
      Pages: 694 - 694
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0683
      Issue No: Vol. 29, No. 6 (2018)
       
  • Phase shifts in protein folding space: links to stress adaptation and
           disease

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      Authors: Alberti, S; Jakob, U.
      Pages: 695 - 695
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0685
      Issue No: Vol. 29, No. 6 (2018)
       
  • Actin dynamics and function

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      Authors: Gupton, S. L; Campellone, K. G.
      Pages: 696 - 697
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E18-01-0010
      Issue No: Vol. 29, No. 6 (2018)
       
  • Fifty years of microtubule sliding in cilia

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      Authors: King, S. M; Sale, W. S.
      Pages: 698 - 701
      Abstract: Motility of cilia (also known as flagella in some eukaryotes) is based on axonemal doublet microtubule sliding that is driven by the dynein molecular motors. Dyneins are organized into intricately patterned inner and outer rows of arms, whose collective activity is to produce inter-microtubule movement. However, to generate a ciliary bend, not all dyneins can be active simultaneously. The switch point model accounts, in part, for how dynein motors are regulated during ciliary movement. On the basis of this model, supported by key direct experimental observations as well as more recent theoretical and structural studies, we are now poised to understand the mechanics of how ciliary dynein coordination controls axonemal bend formation and propagation.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-07-0483
      Issue No: Vol. 29, No. 6 (2018)
       
  • Control of septin filament flexibility and bundling by subunit composition
           and nucleotide interactions

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      Authors: Khan, A; Newby, J, Gladfelter, A. S.
      Pages: 702 - 712
      Abstract: Septins self-assemble into heteromeric rods and filaments to act as scaffolds and modulate membrane properties. How cells tune the biophysical properties of septin filaments to control filament flexibility and length, and in turn the size, shape, and position of higher-order septin structures, is not well understood. We examined how rod composition and nucleotide availability influence physical properties of septins such as annealing, fragmentation, bundling, and bending. We found that septin complexes have symmetric termini, even when both Shs1 and Cdc11 are coexpressed. The relative proportion of Cdc11/Shs1 septin complexes controls the biophysical properties of filaments and influences the rate of annealing, fragmentation, and filament flexibility. Additionally, the presence and apparent exchange of guanine nucleotide also alters filament length and bundling. An Shs1 mutant that is predicted to alter nucleotide hydrolysis has altered filament length and dynamics in cells and impacts cell morphogenesis. These data show that modulating filament properties through rod composition and nucleotide binding can control formation of septin assemblies that have distinct physical properties and functions.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-10-0608
      Issue No: Vol. 29, No. 6 (2018)
       
  • Cdk1-dependent phosphoinhibition of a formin-F-BAR interaction opposes
           cytokinetic contractile ring formation

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      Authors: Willet, A. H; Bohnert, K. A, Gould, K. L.
      Pages: 713 - 721
      Abstract: In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). A single essential formin, Cdc12, localizes to the cell middle upon mitotic onset and nucleates the F-actin of the CR. Cdc12 medial recruitment is mediated in part by its direct binding to the F-BAR scaffold Cdc15. Given that Cdc12 is hyperphosphorylated in M phase, we explored whether Cdc12 phosphoregulation impacts its association with Cdc15 during mitosis. We found that Cdk1, a major mitotic kinase, phosphorylates Cdc12 on six N-terminal residues near the Cdc15-binding site, and phosphorylation on these sites inhibits its interaction with the Cdc15 F-BAR domain. Consistent with this finding, a cdc12 mutant with all six Cdk1 sites changed to phosphomimetic residues (cdc12-6D) displays phenotypes similar to cdc12-P31A, in which the Cdc15-binding motif is disrupted; both show reduced Cdc12 at the CR and delayed CR formation. Together, these results indicate that Cdk1 phosphorylation of formin Cdc12 antagonizes its interaction with Cdc15 and thereby opposes Cdc12’s CR localization. These results are consistent with a general role for Cdk1 in inhibiting cytokinesis until chromosome segregation is complete.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-11-0646
      Issue No: Vol. 29, No. 6 (2018)
       
  • Interaction between the Caenorhabditis elegans centriolar protein SAS-5
           and microtubules facilitates organelle assembly

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      Authors: Bianchi, S; Rogala, K. B, Dynes, N. J, Hilbert, M, Leidel, S. A, Steinmetz, M. O, Gonczy, P, Vakonakis, I.
      Pages: 722 - 735
      Abstract: Centrioles are microtubule-based organelles that organize the microtubule network and seed the formation of cilia and flagella. New centrioles assemble through a stepwise process dependent notably on the centriolar protein SAS-5 in Caenorhabditis elegans. SAS-5 and its functional homologues in other species form oligomers that bind the centriolar proteins SAS-6 and SAS-4, thereby forming an evolutionarily conserved structural core at the onset of organelle assembly. Here, we report a novel interaction of SAS-5 with microtubules. Microtubule binding requires SAS-5 oligomerization and a disordered protein segment that overlaps with the SAS-4 binding site. Combined in vitro and in vivo analysis of select mutants reveals that the SAS-5–microtubule interaction facilitates centriole assembly in C. elegans embryos. Our findings lead us to propose that the interdependence of SAS-5 oligomerization and microtubule binding reflects an avidity mechanism, which also strengthens SAS-5 associations with other centriole components and, thus, promotes organelle assembly.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-06-0412
      Issue No: Vol. 29, No. 6 (2018)
       
  • Two subunits of the exocyst, Sec3p and Exo70p, can function exclusively on
           the plasma membrane

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      Authors: Liu, D; Li, X, Shen, D, Novick, P.
      Pages: 736 - 750
      Abstract: The exocyst is an octameric complex that tethers secretory vesicles to the plasma membrane in preparation for fusion. We anchored each subunit with a transmembrane (TM) domain at its N- or C-terminus. Only N-terminally anchored TM-Sec3p and C-terminally anchored Exo70p-TM proved functional. These findings orient the complex with respect to the membrane and establish that Sec3p and Exo70p can function exclusively on the membrane. The functions of TM-Sec3p and Exo70p-TM were largely unaffected by blocks in endocytic recycling, suggesting that they act on the plasma membrane rather than on secretory vesicles. Cytosolic pools of the other exocyst subunits were unaffected in TM-sec3 cells, while they were partially depleted in exo70-TM cells. Blocking actin-dependent delivery of secretory vesicles in act1-3 cells results in loss of Sec3p from the purified complex. Our results are consistent with a model in which Sec3p and Exo70p can function exclusively on the plasma membrane while the other subunits are brought to them on secretory vesicles.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-08-0518
      Issue No: Vol. 29, No. 6 (2018)
       
  • Constitutive centromere-associated network contacts confer differential
           stability on CENP-A nucleosomes in vitro and in the cell

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      Authors: Cao, S; Zhou, K, Zhang, Z, Luger, K, Straight, A. F.
      Pages: 751 - 762
      Abstract: Eukaryotic centromeres are defined by the presence of nucleosomes containing the histone H3 variant, centromere protein A (CENP-A). Once incorporated at centromeres, CENP-A nucleosomes are remarkably stable, exhibiting no detectable loss or exchange over many cell cycles. It is currently unclear whether this stability is an intrinsic property of CENP-A containing chromatin or whether it arises from proteins that specifically associate with CENP-A chromatin. Two proteins, CENP-C and CENP-N, are known to bind CENP-A human nucleosomes directly. Here we test the hypothesis that CENP-C or CENP-N stabilize CENP-A nucleosomes in vitro and in living cells. We show that CENP-N stabilizes CENP-A nucleosomes alone and additively with CENP-C in vitro. However, removal of CENP-C and CENP-N from cells, or mutating CENP-A so that it no longer interacts with CENP-C or CENP-N, had no effect on centromeric CENP-A stability in vivo. Thus, the stability of CENP-A nucleosomes in chromatin does not arise solely from its interactions with CENP-C or CENP-N.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-10-0596
      Issue No: Vol. 29, No. 6 (2018)
       
  • Differential equation methods for simulation of GFP kinetics in non-steady
           state experiments

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      Authors: Phair; R. D.
      Pages: 763 - 771
      Abstract: Genetically encoded fluorescent proteins, combined with fluorescence microscopy, are widely used in cell biology to collect kinetic data on intracellular trafficking. Methods for extraction of quantitative information from these data are based on the mathematics of diffusion and tracer kinetics. Current methods, although useful and powerful, depend on the assumption that the cellular system being studied is in a steady state, that is, the assumption that all the molecular concentrations and fluxes are constant for the duration of the experiment. Here, we derive new tracer kinetic analytical methods for non–steady state biological systems by constructing mechanistic nonlinear differential equation models of the underlying cell biological processes and linking them to a separate set of differential equations governing the kinetics of the fluorescent tracer. Linking the two sets of equations is based on a new application of the fundamental tracer principle of indistinguishability and, unlike current methods, supports correct dependence of tracer kinetics on cellular dynamics. This approach thus provides a general mathematical framework for applications of GFP fluorescence microscopy (including photobleaching [FRAP, FLIP] and photoactivation to frequently encountered experimental protocols involving physiological or pharmacological perturbations (e.g., growth factors, neurotransmitters, acute knockouts, inhibitors, hormones, cytokines, and metabolites) that initiate mechanistically informative intracellular transients. When a new steady state is achieved, these methods automatically reduce to classical steady state tracer kinetic analysis.
      PubDate: 2018-03-13T10:36:57-07:00
      DOI: 10.1091/mbc.E17-06-0396
      Issue No: Vol. 29, No. 6 (2018)
       
 
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