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  • *Vesicular Transport Proteins  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1998-07-31
    Description: Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Springer, S -- Schekman, R -- New York, N.Y. -- Science. 1998 Jul 31;281(5377):698-700.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720-3202, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9685263" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; COP-Coated Vesicles ; Carrier Proteins/*metabolism ; Endoplasmic Reticulum/*metabolism ; Fungal Proteins/*metabolism ; GTP Phosphohydrolases/metabolism ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; Golgi Apparatus/*metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Guanylyl Imidodiphosphate/metabolism/pharmacology ; Membrane Proteins/*metabolism ; *Membrane Transport Proteins ; *Monomeric GTP-Binding Proteins ; Qb-SNARE Proteins ; Qc-SNARE Proteins ; R-SNARE Proteins ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; SNARE Proteins ; Saccharomyces cerevisiae ; *Saccharomyces cerevisiae Proteins ; *Vesicular Transport Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-01-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Marcus C S -- Schekman, Randy -- New York, N.Y. -- Science. 2004 Jan 23;303(5657):479-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14739445" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/chemistry/metabolism ; Adaptor Proteins, Vesicular Transport ; Animals ; COP-Coated Vesicles/metabolism ; Carrier Proteins/chemistry/metabolism ; Cell Membrane/chemistry/*metabolism/ultrastructure ; Clathrin/metabolism ; Coated Vesicles/chemistry/metabolism/ultrastructure ; Cytoplasmic Vesicles/chemistry/*metabolism/ultrastructure ; Dimerization ; Drosophila/chemistry ; Drosophila Proteins/*chemistry/metabolism/physiology ; Dynamins/metabolism ; Endocytosis ; Exocytosis ; GTPase-Activating Proteins/chemistry/metabolism ; Nerve Tissue Proteins/*chemistry/*metabolism/physiology ; Neuropeptides/chemistry/metabolism ; Protein Binding ; Protein Structure, Secondary ; *Protein Structure, Tertiary ; *Vesicular Transport Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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