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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2013-05-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Min -- Schekman, Randy -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 May 3;340(6132):559-61. doi: 10.1126/science.1234740.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720-3370, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23641104" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autophagy ; Carrier Proteins/metabolism ; Cell Membrane/metabolism/*secretion ; Exosomes/metabolism ; Lysosomes/metabolism ; Membrane Fusion ; Membrane Proteins/metabolism ; Membrane Transport Proteins/metabolism ; Models, Biological ; Phagosomes/metabolism ; Proteins/*metabolism/*secretion ; *Secretory Pathway ; Secretory Vesicles/metabolism
    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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  • 3
    Publication Date: 2012-02-24
    Description: Packaging of proteins from the endoplasmic reticulum into COPII vesicles is essential for secretion. In cells, most COPII vesicles are approximately 60-80 nm in diameter, yet some must increase their size to accommodate 300-400 nm procollagen fibres or chylomicrons. Impaired COPII function results in collagen deposition defects, cranio-lenticulo-sutural dysplasia, or chylomicron retention disease, but mechanisms to enlarge COPII coats have remained elusive. Here, we identified the ubiquitin ligase CUL3-KLHL12 as a regulator of COPII coat formation. CUL3-KLHL12 catalyses the monoubiquitylation of the COPII-component SEC31 and drives the assembly of large COPII coats. As a result, ubiquitylation by CUL3-KLHL12 is essential for collagen export, yet less important for the transport of small cargo. We conclude that monoubiquitylation controls the size and function of a vesicle coat.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292188/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292188/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jin, Lingyan -- Pahuja, Kanika Bajaj -- Wickliffe, Katherine E -- Gorur, Amita -- Baumgartel, Christine -- Schekman, Randy -- Rape, Michael -- DP2 OD003088/OD/NIH HHS/ -- DP2 OD003088-01/OD/NIH HHS/ -- R01 GM083064/GM/NIGMS NIH HHS/ -- R01 GM083064-04/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Feb 22;482(7386):495-500. doi: 10.1038/nature10822.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California at Berkeley, California 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22358839" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COP-Coated Vesicles/*chemistry/*metabolism ; Cell Line ; Cell Shape ; Collagen/metabolism ; Cullin Proteins/genetics/metabolism ; Embryonic Stem Cells/cytology/metabolism ; HeLa Cells ; Humans ; Mice ; Microfilament Proteins/genetics/metabolism ; Protein Transport ; Ubiquitin/*metabolism ; Ubiquitination ; Vesicular Transport Proteins/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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