ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Systems survey of endocytosis by multiparametric image analysis (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-03-02
    Description: Endocytosis is a complex process fulfilling many cellular and developmental functions. Understanding how it is regulated and integrated with other cellular processes requires a comprehensive analysis of its molecular constituents and general design principles. Here, we developed a new strategy to phenotypically profile the human genome with respect to transferrin (TF) and epidermal growth factor (EGF) endocytosis by combining RNA interference, automated high-resolution confocal microscopy, quantitative multiparametric image analysis and high-performance computing. We identified several novel components of endocytic trafficking, including genes implicated in human diseases. We found that signalling pathways such as Wnt, integrin/cell adhesion, transforming growth factor (TGF)-beta and Notch regulate the endocytic system, and identified new genes involved in cargo sorting to a subset of signalling endosomes. A systems analysis by Bayesian networks further showed that the number, size, concentration of cargo and intracellular position of endosomes are not determined randomly but are subject to specific regulation, thus uncovering novel properties of the endocytic system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collinet, Claudio -- Stoter, Martin -- Bradshaw, Charles R -- Samusik, Nikolay -- Rink, Jochen C -- Kenski, Denise -- Habermann, Bianca -- Buchholz, Frank -- Henschel, Robert -- Mueller, Matthias S -- Nagel, Wolfgang E -- Fava, Eugenio -- Kalaidzidis, Yannis -- Zerial, Marino -- England -- Nature. 2010 Mar 11;464(7286):243-9. doi: 10.1038/nature08779. Epub 2010 Feb 28.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Molecular Cell Biology and Genetics, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20190736" target="_blank"〉PubMed〈/a〉
    Keywords: Computing Methodologies ; Endocytosis/*physiology ; Endosomes/metabolism ; Epidermal Growth Factor/metabolism ; Gene Expression Profiling/*methods ; Genome-Wide Association Study ; Humans ; *Image Processing, Computer-Assisted ; Metabolic Networks and Pathways/physiology ; Microscopy, Confocal ; Phenotype ; Protein Transport/physiology ; RNA Interference ; Signal Transduction/physiology ; Transferrin/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-05-22
    Description: Rab GTPases and SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are evolutionarily conserved essential components of the eukaryotic intracellular transport system. Although pairing of cognate SNAREs is sufficient to fuse membranes in vitro, a complete reconstitution of the Rab-SNARE machinery has never been achieved. Here we report the reconstitution of the early endosomal canine Rab5 GTPase, its key regulators and effectors together with SNAREs into proteoliposomes using a set of 17 recombinant human proteins. These vesicles behave like minimal 'synthetic' endosomes, fusing with purified early endosomes or with each other in vitro. Membrane fusion measured by content-mixing and morphological assays requires the cooperativity between Rab5 effectors and cognate SNAREs which, together, form a more efficient 'core machinery' than SNAREs alone. In reconstituting a fusion mechanism dependent on both a Rab GTPase and SNAREs, our work shows that the two machineries act coordinately to increase the specificity and efficiency of the membrane tethering and fusion process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohya, Takeshi -- Miaczynska, Marta -- Coskun, Unal -- Lommer, Barbara -- Runge, Anja -- Drechsel, David -- Kalaidzidis, Yannis -- Zerial, Marino -- England -- Nature. 2009 Jun 25;459(7250):1091-7. doi: 10.1038/nature08107. Epub 2009 May 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19458617" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cricetinae ; Cytosol/metabolism ; Dogs ; Endosomes/metabolism/*physiology ; Humans ; Membrane Fusion/*physiology ; Microscopy, Electron ; Proteolipids/metabolism/ultrastructure ; Recombinant Proteins/metabolism ; SNARE Proteins/*metabolism ; Vesicular Transport Proteins/metabolism ; rab GTP-Binding Proteins/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Kinetics of morphogen gradient formation (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-01-27
    Description: In the developing fly wing, secreted morphogens such as Decapentaplegic (Dpp) and Wingless (Wg) form gradients of concentration providing positional information. Dpp forms a longer-range gradient than Wg. To understand how the range is controlled, we measured the four key kinetic parameters governing morphogen spreading: the production rate, the effective diffusion coefficient, the degradation rate, and the immobile fraction. The four parameters had different values for Dpp versus Wg. In addition, Dynamin-dependent endocytosis was required for spreading of Dpp, but not Wg. Thus, the cellular mechanisms of Dpp and Wingless spreading are different: Dpp spreading requires endocytic, intracellular trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kicheva, Anna -- Pantazis, Periklis -- Bollenbach, Tobias -- Kalaidzidis, Yannis -- Bittig, Thomas -- Julicher, Frank -- Gonzalez-Gaitan, Marcos -- New York, N.Y. -- Science. 2007 Jan 26;315(5811):521-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauer Strasse 108, 01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17255514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Diffusion ; Drosophila Proteins/*metabolism ; Drosophila melanogaster/growth & development/*metabolism ; Endocytosis ; Fluorescence Recovery After Photobleaching ; Kinetics ; Mathematics ; Proto-Oncogene Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Temperature ; Wings, Animal/*growth & development/*metabolism ; Wnt1 Protein
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...