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Cover image for Vol. 15 Issue 11

Edited By: Michael S. Marks, Mark C. P. Marsh, Trina A. Schroer, Tom H. Stevens

Online ISSN: 1600-0854

Highlights

  • ORIGINAL ARTICLE: Src Regulates Sequence-Dependent Beta-2 Adrenergic Receptor Recycling via Cortactin Phosphorylation

    ORIGINAL ARTICLE: Src Regulates Sequence‐Dependent Beta‐2 Adrenergic Receptor Recycling via Cortactin Phosphorylation

    Model for heterologous control of the sequence-dependent recycling pathway by Src. Signaling receptors such as the beta-2 adrenergic receptor, a prototypic GPCR, are segregated from bulk recycling proteins like the TfR in the endosome and sorted into specialized sequence-dependent recycling microdomains. These microdomains are marked by a specialized protein machinery including a dynamic actin cytoskeleton. Src signaling, via phosphorylation of cortactin at Y466, regulates the rate of membrane scission from these microdomains, and therefore the rate of receptor delivery to the cell surface. This allows for specific control over sequence-dependent recycling without affecting bulk recycling.

  • ORIGINAL ARTICLE: Vmp1 Regulates PtdIns3P Signaling During Autophagosome Formation in Dictyostelium discoideum

    ORIGINAL ARTICLE: Vmp1 Regulates PtdIns3P Signaling During Autophagosome Formation in Dictyostelium discoideum

    The pattern of GFP-Atg18 in the vmp1− mutant suggests a defect in an early stage of autophagosome formation. A) Dictyostelium cells expressing GFP-Atg18 and Vmp1-RFP were imaged by time-lapse confocal fluorescence to show colocalization. B) Wild-type and mutant cells expressing the autophagosome marker GFP-Atg18 were analysed by confocal microscopy during growth in HL5 and starvation in PDF for 30 min. Maximum intensity projections of 10 z-optical sections are shown. B) Sequential z-sections of the cell labeled by and asterisk in panel B showing an abnormal ring-like feature. Bars: 10 µm.

  • ORIGINAL ARTICLE: Targeting of Viral Capsids to Nuclear Pores in a Cell-Free Reconstitution System

    ORIGINAL ARTICLE: Targeting of Viral Capsids to Nuclear Pores in a Cell-Free Reconstitution System

    Targeting of HSV1 capsids to NPCs on Xenopus nuclei in vitro. A–C). Functional (A), Imp β45–462 (B) or BAPTA (C) nuclei were reconstituted in vitro. Completion of nuclear assembly was monitored by epi-fluorescence microscopy by DNA staining with Hoechst 33258 (i and iii), NPC staining with fluorescently labeled mAb414 (ii) and the transport capacity of the assembled NPCs was confirmed by the nuclear import of TRITC-NLS-BSA (iv). Scale bar: 10 µm. D,E) Binding of viral 0.5 m KCl capsids extracted from extracellular particles of HSV1-GFPVP26 (ii and iii, green, white arrowheads) to Xenopus nuclei was analyzed using confocal fluorescence laser scanning microscopy and a serial z-slicing of 0.37 µm optical sections. A surface view (D) and one midsection (E) of a representative nucleus are shown. NPCs were labeled with Imp β45–462-TRITC (i and iii, red). Scale bar: 10 µm. F,G) HSV1-GFPVP26 viral 0.5 m capsids were incubated with Xenopus nuclei harboring functional NPCs for 45 min, labeled with a polyclonal rabbit antiserum raised against intact HSV1 capsids (Remus, bleed V) and colloidal gold with a diameter of 12 nm coated with anti-rabbit antibodies. The specimens were analyzed by field emission scanning electron microscopy. F) 3D surface topography of reconstituted nuclei from different views in the in-lens images (i–iii). The same areas were imaged through a backscatter electron detector revealing the positions of gold-conjugated antibodies (Gi–iii; inverted color mode). HSV1 capsids (white arrowheads) are bound to the cytoplasmic face of the NPCs (white arrows). Scale bar: 100 nm.

  • ORIGINAL ARTICLE : Arabinogalactan Glycosyltransferases Target to a Unique Subcellular Compartment That May Function in Unconventional Secretion in Plants

    ORIGINAL ARTICLE : Arabinogalactan Glycosyltransferases Target to a Unique Subcellular Compartment That May Function in Unconventional Secretion in Plants

    The subcellular localization ofAtGlcAT14A-mCer3. AtGlcAT14A-mCer3 (A–I, green) was coexpressed with GnTI-mRFP (A–C, magenta), GMII-mRFP (D–F, magenta) and ST-YFP (G–I, magenta) in N. benthamiana leaves. AtGlcAT14A-mCer3 colocalized with GnTI-mRFP, GMII-mRFP and ST-YFP in the Golgi compartments (overlapping signals, A–I) but was also found alone in the small compartments, indicated by arrowheads. Scale bars = 10 µm.

  • ORIGINAL ARTICLE: Nucleoli and Stress Granules: Connecting Distant Relatives

    ORIGINAL ARTICLE: Nucleoli and Stress Granules: Connecting Distant Relatives

    Localization of nucleolar andSGproteins in stressed mammalian cells. HeLa cells were treated with sodium arsenite, a compound that induces oxidative stress, and proteins were detected by immunofluorescence staining. Nucleostemin (magenta) is a marker for nucleoli, whereas G3BP1 (yellow) associates with SGs. Note that the RNA-binding protein hnRNP K (green) is present in both compartments. Surface rendering was performed on confocal image stacks; size bar is 5 µm (A). Magnified views of a nucleolus (B), the nucleolar interior (C) or one of the SGs (D).

  • ORIGINAL ARTICLE: Src Regulates Sequence‐Dependent Beta‐2 Adrenergic Receptor Recycling via Cortactin Phosphorylation
  • ORIGINAL ARTICLE: Vmp1 Regulates PtdIns3P Signaling During Autophagosome Formation in Dictyostelium discoideum
  • ORIGINAL ARTICLE: Targeting of Viral Capsids to Nuclear Pores in a Cell-Free Reconstitution System
  • ORIGINAL ARTICLE : Arabinogalactan Glycosyltransferases Target to a Unique Subcellular Compartment That May Function in Unconventional Secretion in Plants
  • ORIGINAL ARTICLE: Nucleoli and Stress Granules: Connecting Distant Relatives

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Rab5 and Ndfip1 Are Involved in Pten Ubiquitination and Nuclear Trafficking
Yijia Li, Ley-Hian Low, Ulrich Putz, Choo-Peng Goh, Seong-Seng Tan and Jason Howitt

Depending on its localization, Pten (the central antagonist of PI3K signaling in the cytoplasm) is involved in many diverse cellular functions including controlling mitosis and DNA repair, cellular homeostasis, cell migration and/or cell proliferation. Balancing the cellular distribution of Pten is crucial to the function of the cell. Li and colleagues provide evidence that sorting of Pten to various organelles occurs in endosomes. Using bimolecular fluorescence complementation and dominant negative Rab5, they demonstrate that Rab5 and the E3 ligase adaptor protein Ndfip1 work together in to ubiquitinate Pten, which is required for its trafficking to the nucleus.


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