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  • American Society for Cell Biology (ASCB)  (8)
  • 1
    Online Resource
    Online Resource
    Role of Insulin-dependent Cortical Fodrin/Spectrin Remodeling in Glucose Transporter 4 Translocation in Rat Adipocytes
    American Society for Cell Biology (ASCB) ; 2006
    In:  Molecular Biology of the Cell Vol. 17, No. 10 ( 2006-10), p. 4249-4256
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 17, No. 10 ( 2006-10), p. 4249-4256
    Abstract: Fodrin or nonerythroid spectrin is an abundant component of the cortical cytoskeletal network in rat adipocytes. Fodrin has a highly punctate distribution in resting cells, and insulin causes a dramatic remodeling of fodrin to a more diffuse pattern. Insulin-mediated remodeling of actin occurs to a lesser extent than does that of fodrin. We show that fodrin interacts with the t-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 4, and this interaction is increased by insulin stimulation and decreased by prior latrunculin A treatment. Latrunculin A disrupts all actin filaments, inhibits glucose transporter 4 (GLUT4) translocation, and causes fodrin to partially redistribute from the plasma membrane to the cytosol. In contrast, cytochalasin D disrupts only the short actin filament signal, and cytochalasin D neither inhibits GLUT4 translocation nor fodrin redistribution in adipocytes. Together, our data suggest that insulin induces remodeling of the fodrin–actin network, which is required for the fusion of GLUT4 storage vesicles with the plasma membrane by permitting their access to the t-SNARE syntaxin 4.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e06-04-0278
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2006
    detail.hit.zdb_id: 1474922-1
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  • 2
    Online Resource
    Online Resource
    Proteome-wide quantitative multiplexed profiling of protein expression: carbon-source dependency in Saccharomyces cerevisiae
    American Society for Cell Biology (ASCB) ; 2015
    In:  Molecular Biology of the Cell Vol. 26, No. 22 ( 2015-11-05), p. 4063-4074
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 26, No. 22 ( 2015-11-05), p. 4063-4074
    Abstract: The global proteomic alterations in the budding yeast Saccharomyces cerevisiae due to differences in carbon sources can be comprehensively examined using mass spectrometry–based multiplexing strategies. In this study, we investigate changes in the S. cerevisiae proteome resulting from cultures grown in minimal media using galactose, glucose, or raffinose as the carbon source. We used a tandem mass tag 9-plex strategy to determine alterations in relative protein abundance due to a particular carbon source, in triplicate, thereby permitting subsequent statistical analyses. We quantified more than 4700 proteins across all nine samples; 1003 proteins demonstrated statistically significant differences in abundance in at least one condition. The majority of altered proteins were classified as functioning in metabolic processes and as having cellular origins of plasma membrane and mitochondria. In contrast, proteins remaining relatively unchanged in abundance included those having nucleic acid–related processes, such as transcription and RNA processing. In addition, the comprehensiveness of the data set enabled the analysis of subsets of functionally related proteins, such as phosphatases, kinases, and transcription factors. As a resource, these data can be mined further in efforts to understand better the roles of carbon source fermentation in yeast metabolic pathways and the alterations observed therein, potentially for industrial applications, such as biofuel feedstock production.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.E15-07-0499
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2015
    detail.hit.zdb_id: 1474922-1
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  • 3
    Online Resource
    Online Resource
    An FTS/Hook/p107 FHIP Complex Interacts with and Promotes Endosomal Clustering by the Homotypic Vacuolar Protein Sorting Complex
    American Society for Cell Biology (ASCB) ; 2008
    In:  Molecular Biology of the Cell Vol. 19, No. 12 ( 2008-12), p. 5059-5071
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 19, No. 12 ( 2008-12), p. 5059-5071
    Abstract: Fused Toes (FTS) is a member of a small group of inactive variant E2 ubiquitin-conjugating enzyme domain-containing proteins of unknown function. Through proteomic analysis of FTS complexes purified from human embryonic kidney 293T cells, we identified a new multiprotein complex, the FHF complex, containing FTS, members of the microtubule-binding Hook family of coiled-coil proteins (Hook1, Hook2, and Hook3), and a previously uncharacterized 107-kDa protein, FTS and Hook Interacting Protein (FHIP). FTS associated with a conserved C-terminal motif in Hook proteins in the yeast two-hybrid system and in tissue culture cells, and Hook proteins were found to form homo- and heterodimers. The ∼500-kDa FHF complex contained all three Hook proteins, and small interfering RNA depletion experiments suggest that Hook proteins can interact interchangeably within this complex. Hook proteins as well as FTS interact with members of both the class B and class C components of the homotypic vesicular protein sorting (HOPS) complex. Depletion of FTS by RNA interference affects both the trafficking of epidermal growth factor from early-to-late endosome/lysosomes and the efficiency by which overexpression of the HOPS component Vps18 promotes clustering of lysosomal-associated membrane protein 1-positive endosome/lysosomes. These data suggest that the FTS/Hook/FHIP complex functions to promote vesicle trafficking and/or fusion via the HOPS complex.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e08-05-0473
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2008
    detail.hit.zdb_id: 1474922-1
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  • 4
    Online Resource
    Online Resource
    Phosphorylation Controls Autoinhibition of Cytoplasmic Linker Protein-170
    American Society for Cell Biology (ASCB) ; 2010
    In:  Molecular Biology of the Cell Vol. 21, No. 15 ( 2010-08), p. 2661-2673
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 21, No. 15 ( 2010-08), p. 2661-2673
    Abstract: Cytoplasmic linker protein (CLIP)-170 is a microtubule (MT) plus-end-tracking protein that regulates MT dynamics and links MT plus ends to different intracellular structures. We have shown previously that intramolecular association between the N and C termini results in autoinhibition of CLIP-170, thus altering its binding to MTs and the dynactin subunit p150 Glued (J. Cell Biol. 2004: 166, 1003–1014). In this study, we demonstrate that conformational changes in CLIP-170 are regulated by phosphorylation that enhances the affinity between the N- and C-terminal domains. By using site-directed mutagenesis and phosphoproteomic analysis, we mapped the phosphorylation sites in the third serine-rich region of CLIP-170. A phosphorylation-deficient mutant of CLIP-170 displays an “open” conformation and a higher binding affinity for growing MT ends and p150 Glued as compared with nonmutated protein, whereas a phosphomimetic mutant confined to the “folded back” conformation shows decreased MT association and does not interact with p150 Glued . We conclude that phosphorylation regulates CLIP-170 conformational changes resulting in its autoinhibition.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e09-12-1036
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2010
    detail.hit.zdb_id: 1474922-1
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  • 5
    Online Resource
    Online Resource
    Intramolecular interactions control Vms1 translocation to damaged mitochondria
    American Society for Cell Biology (ASCB) ; 2013
    In:  Molecular Biology of the Cell Vol. 24, No. 9 ( 2013-05), p. 1263-1273
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 24, No. 9 ( 2013-05), p. 1263-1273
    Abstract: Mitochondrial dysfunction is associated with the development of many age-related human diseases. Therefore recognizing and correcting the early signs of malfunctioning mitochondria is of critical importance for cellular welfare and survival. We previously demonstrated that VCP/Cdc48-associated mitochondrial stress responsive 1 (Vms1) is a component of a mitochondrial surveillance system that mediates the stress-responsive degradation of mitochondrial proteins by the proteasome. Here we propose novel mechanisms through which Vms1 monitors the status of mitochondria and is recruited to damaged or stressed mitochondria. We find that Vms1 contains a highly conserved region that is necessary and sufficient for mitochondrial targeting (the mitochondrial targeting domain [MTD]). Of interest, MTD-mediated mitochondrial targeting of Vms1 is negatively regulated by a direct interaction with the Vms1 N-terminus. Using laser-induced generation of mitochondrial reactive oxygen species, we also show that Vms1 is preferentially recruited to mitochondria subjected to oxidative stress. These studies define cellular and biochemical mechanisms by which Vms1 locali­zation to mitochondria is controlled to enable an efficient protein quality control system.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e13-02-0072
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2013
    detail.hit.zdb_id: 1474922-1
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  • 6
    Online Resource
    Online Resource
    The γTuRC Revisited: A Comparative Analysis of Interphase and Mitotic Human γTuRC Redefines the Set of Core Components and Identifies the Novel Subunit GCP8
    American Society for Cell Biology (ASCB) ; 2010
    In:  Molecular Biology of the Cell Vol. 21, No. 22 ( 2010-11-15), p. 3963-3972
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 21, No. 22 ( 2010-11-15), p. 3963-3972
    Abstract: The γ-tubulin complex is a multi-subunit protein complex that nucleates microtubule polymerization. γ-Tubulin complexes are present in all eukaryotes, but size and subunit composition vary. In Drosophila, Xenopus, and humans large γ-tubulin ring complexes (γTuRCs) have been described, which have a characteristic open ring-shaped structure and are composed of a similar set of subunits, named γ-tubulin, GCPs 2-6, and GCP-WD in humans. Despite the identification of these proteins, γTuRC function and regulation remain poorly understood. Here we establish a new method for the purification of native human γTuRC. Using mass spectrometry of whole protein mixtures we compared the composition of γTuRCs from nonsynchronized and mitotic human cells. Based on our analysis we can define core subunits as well as more transient interactors such as the augmin complex, which associates specifically with mitotic γTuRCs. We also identified GCP8/MOZART2 as a novel core subunit that is present in both interphase and mitotic γTuRCs. GCP8 depletion does not affect γTuRC assembly but interferes with γTuRC recruitment and microtubule nucleation at interphase centrosomes without disrupting general centrosome structure. GCP8-depleted cells do not display any obvious mitotic defects, suggesting that GCP8 specifically affects the organization of the interphase microtubule network.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e10-05-0408
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2010
    detail.hit.zdb_id: 1474922-1
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  • 7
    Online Resource
    Online Resource
    A phosphatase threshold sets the level of Cdk1 activity in early mitosis in budding yeast
    American Society for Cell Biology (ASCB) ; 2011
    In:  Molecular Biology of the Cell Vol. 22, No. 19 ( 2011-10), p. 3595-3608
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 22, No. 19 ( 2011-10), p. 3595-3608
    Abstract: Entry into mitosis is initiated by synthesis of cyclins, which bind and activate cyclin-dependent kinase 1 (Cdk1). Cyclin synthesis is gradual, yet activation of Cdk1 occurs in a stepwise manner: a low level of Cdk1 activity is initially generated that triggers early mitotic events, which is followed by full activation of Cdk1. Little is known about how stepwise activation of Cdk1 is achieved. A key regulator of Cdk1 is the Wee1 kinase, which phosphorylates and inhibits Cdk1. Wee1 and Cdk1 show mutual regulation: Cdk1 phosphorylates Wee1, which activates Wee1 to inhibit Cdk1. Further phosphorylation events inactivate Wee1. We discovered that a specific form of protein phosphatase 2A (PP2A Cdc55 ) opposes the initial phosphorylation of Wee1 by Cdk1. In vivo analysis, in vitro reconstitution, and mathematical modeling suggest that PP2A Cdc55 sets a threshold that limits activation of Wee1, thereby allowing a low constant level of Cdk1 activity to escape Wee1 inhibition in early mitosis. These results define a new role for PP2A Cdc55 and reveal a systems-level mechanism by which dynamically opposed kinase and phosphatase activities can modulate signal strength.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e11-04-0340
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2011
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  • 8
    Online Resource
    Online Resource
    Mapping and analysis of phosphorylation sites: a quick guide for cell biologists
    American Society for Cell Biology (ASCB) ; 2013
    In:  Molecular Biology of the Cell Vol. 24, No. 5 ( 2013-03), p. 535-542
    Details
    In: Molecular Biology of the Cell, American Society for Cell Biology (ASCB), Vol. 24, No. 5 ( 2013-03), p. 535-542
    Abstract: A mechanistic understanding of signaling networks requires identification and analysis of phosphorylation sites. Mass spectrometry offers a rapid and highly sensitive approach to mapping phosphorylation sites. However, mass spectrometry has significant limitations that must be considered when planning to carry out phosphorylation-site mapping. Here we provide an overview of key information that should be taken into consideration before beginning phosphorylation-site analysis, as well as a step-by-step guide for carrying out successful experiments.
    Type of Medium: Online Resource
    ISSN: 1059-1524 , 1939-4586
    URL: Article
    DOI: 10.1091/mbc.e12-09-0677
    Language: English
    Publisher: American Society for Cell Biology (ASCB)
    Publication Date: 2013
    detail.hit.zdb_id: 1474922-1
    SSG: 12
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