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  • 1. Bai, Ming
    et al.
    Gad, Helge
    Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
    Turacchio, Gabriele
    Cocucci, Emanuele
    Yang, Jia-Shu
    Li, Jian
    Beznoussenko, Galina V.
    Nie, Zhongzhen
    Luo, Ruibai
    Fu, Lianwu
    Collawn, James F.
    Kirchhausen, Tomas
    Luini, Alberto
    Hsu, Victor W.
    ARFGAP1 promotes AP-2-dependent endocytosis2011In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 13, no 5, p. 559-U144Article in journal (Refereed)
    Abstract [en]

    COPI (coat protein I) and the clathrin-AP-2 (adaptor protein 2) complex are well-characterized coat proteins, but a component that is common to these two coats has not been identified. The GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), ARFGAP1, is a known component of the COPI complex. Here, we show that distinct regions of ARFGAP1 interact with AP-2 and coatomer (components of the COPI complex). Selectively disrupting the interaction of ARFGAP1 with either of these two coat proteins leads to selective inhibition in the corresponding transport pathway. The role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport.

  • 2.
    Hosono, Chie
    et al.
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Matsuda, Ryo
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
    Adryan, Boris
    Samakovlis, Christos
    Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute. ECCPS, University of Giessen, Germany.
    Transient junction anisotropies orient annular cell polarization in the Drosophila airway tubes2015In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 17, no 12, p. 1569-1576Article in journal (Refereed)
    Abstract [en]

    In contrast to planes, three-dimensional (3D) structures such as tubes are physically anisotropic. Tubular organs exhibit a striking orientation of landmarks according to the physical anisotropy of the 3D shape(1-4), in addition to planar cell polarization(5,6). However, the influence of 3D tissue topography on the constituting cells remains underexplored(7-9). Here, we identify a regulatory network polarizing cellular biochemistry according to the physical anisotropy of the 3D tube geometry (tube cell polarization) by a genome-wide, tissue-specific RNAi screen. During Drosophila airway remodelling, each apical cellular junction is equipotent to establish perpendicular actomyosin cables, irrespective of the longitudinal or transverse tube axis. A dynamic transverse enrichment of atypical protein kinase C (aPKC) shifts the balance and transiently targets activated small GTPase RhoA, myosin phosphorylation and Rab11 vesicle trafficking to longitudinal junctions. We propose that the PAR complex translates tube physical anisotropy into longitudinal junctional anisotropy, where cell cell communication aligns the contractile cytoskeleton of neighbouring cells.

  • 3. Stoldt, Stefan
    et al.
    Wenzel, Dirk
    Kehrein, Kirsten
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Riedel, Dietmar
    Ott, Martin
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Jakobs, Stefan
    Spatial orchestration of mitochondrial translation and OXPHOS complex assembly2018In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 20, no 5, p. 528-534Article in journal (Refereed)
    Abstract [en]

    Oxidative phosphorylation (OXPHOS) is vital for the regeneration of the vast majority of ATP in eukaryotic cells(1). OXPHOS is carried out by large multi-subunit protein complexes in the cristae membranes, which are invaginations of the mitochondrial inner membrane. The OXPHOS complexes are a mix of subunits encoded in the nuclear and mitochondrial genomes. Thus, the assembly of these dual-origin complexes is an enormous logistical challenge for the cell. Using super-resolution microscopy (nanoscopy) and quantitative cryo-immunogold electron microscopy, we determined where specific transcripts are translated and where distinct assembly steps of the dual-origin complexes in the yeast Saccharomyces cerevisiae occur. Our data indicate that the mitochondrially encoded proteins of complex III and complex IV are preferentially inserted in different sites of the inner membrane than those of complex V. We further demonstrate that the early, but not the late, assembly steps of complex III and complex IV occur preferentially in the inner boundary membrane. By contrast, all steps of complex V assembly occur mainly in the cristae membranes. Thus, OXPHOS complex assembly is spatially well orchestrated, probably representing an unappreciated regulatory layer in mitochondrial biogenesis.

  • 4.
    Tiklová, Katarína
    et al.
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Senti, Kirsten-André
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Wang, Shenqiu
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Gräslund, Astrid
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Samakovlis, Christos
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Epithelial septate junction assembly relies on melanotransferrin iron binding and endocytosis in Drosophila2010In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 12, no 11, p. 1071-1077Article in journal (Refereed)
    Abstract [en]

    Iron is an essential element in many biological processes. In vertebrates, serum transferrin is the major supplier of iron to tissues, but the function of additional transferrin-like proteins remains poorly understood. Melanotransferrin (MTf) is a phylogenetically conserved, iron-binding epithelial protein. Elevated MTf levels have been implicated in melanoma pathogenesis. Here, we present a functional analysis of MTf in Drosophila melanogaster. Similarly to its human homologue, Drosophila MTf is a lipid-modified, iron-binding protein attached to epithelial cell membranes, and is a component of the septate junctions that form the paracellular permeability barrier in epithelial tissues. We demonstrate that septate junction assembly during epithelial maturation relies on endocytosis and apicolateral recycling of iron-bound MTf. Mouse MTf complements the defects of Drosophila MTf mutants. Drosophila provides the first genetic model for the functional dissection of MTf in epithelial junction assembly and morphogenesis.

  • 5.
    Wang, Shenqiu
    et al.
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Tsarouhas, Vasilis
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Xylourgidis, Nikos
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Sabri, Nafiseh
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Tiklová, Katarína
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Nautiyal, Naumi
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Gallio, Marco
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    Samakovlis, Christos
    Stockholm University, Faculty of Science, The Wenner-Gren Institute .
    The tyrosine kinase Stitcher activates Grainy head and epidermal woundhealing in Drosophila.2009In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 11, no 7, p. 890-895Article in journal (Refereed)
    Abstract [en]

    Epidermal injury initiates a cascade of inflammation, epithelial remodelling and integument repair at wound sites. The regeneration of the extracellular barrier and damaged tissue repair rely on the precise orchestration of epithelial responses triggered by the injury1, 2. Grainy head (Grh) transcription factors induce gene expression to crosslink the extracellular barrier in wounded flies and mice3, 4. However, the activation mechanisms and functions of Grh factors in re-epithelialization remain unknown. Here we identify stitcher (stit), a new Grh target in Drosophila melanogaster. stit encodes a Ret-family receptor tyrosine kinase required for efficient epidermal wound healing. Live imaging analysis reveals that Stit promotes actin cable assembly during wound re-epithelialization. Stit activation also induces extracellular signal-regulated kinase (ERK) phosphorylation along with the Grh-dependent expression of stit and barrier repair genes at the wound sites. The transcriptional stimulation of stit on injury triggers a positive feedback loop increasing the magnitude of epithelial responses. Thus, Stit activation upon wounding coordinates cytoskeletal rearrangements and the level of Grh-mediated transcriptional wound responses.

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