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  • 1
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    Misfolded proteins partition between two distinct quality control compartments (2008)
    Nature Publishing Group (NPG)
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    Publication Date: 2008-08-30
    Description: The accumulation of misfolded proteins in intracellular amyloid inclusions, typical of many neurodegenerative disorders including Huntington's and prion disease, is thought to occur after failure of the cellular protein quality control mechanisms. Here we examine the formation of misfolded protein inclusions in the eukaryotic cytosol of yeast and mammalian cell culture models. We identify two intracellular compartments for the sequestration of misfolded cytosolic proteins. Partition of quality control substrates to either compartment seems to depend on their ubiquitination status and aggregation state. Soluble ubiquitinated misfolded proteins accumulate in a juxtanuclear compartment where proteasomes are concentrated. In contrast, terminally aggregated proteins are sequestered in a perivacuolar inclusion. Notably, disease-associated Huntingtin and prion proteins are preferentially directed to the perivacuolar compartment. Enhancing ubiquitination of a prion protein suffices to promote its delivery to the juxtanuclear inclusion. Our findings provide a framework for understanding the preferential accumulation of amyloidogenic proteins in inclusions linked to human disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746971/" 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/PMC2746971/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaganovich, Daniel -- Kopito, Ron -- Frydman, Judith -- R01 GM056433/GM/NIGMS NIH HHS/ -- R01 GM056433-03/GM/NIGMS NIH HHS/ -- R01 GM056433-04/GM/NIGMS NIH HHS/ -- R01 GM056433-05/GM/NIGMS NIH HHS/ -- R01 GM056433-06/GM/NIGMS NIH HHS/ -- R01 GM056433-07/GM/NIGMS NIH HHS/ -- R01 GM056433-08/GM/NIGMS NIH HHS/ -- R01 NS042842/NS/NINDS NIH HHS/ -- R01 NS042842-07/NS/NINDS NIH HHS/ -- England -- Nature. 2008 Aug 28;454(7208):1088-95. doi: 10.1038/nature07195.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and BioX Program, Stanford University, Stanford, California 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18756251" target="_blank"〉PubMed〈/a〉
    Keywords: Cytosol/metabolism ; HeLa Cells ; Humans ; Prions/metabolism ; Proteasome Endopeptidase Complex/metabolism ; *Protein Folding ; Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/cytology/genetics/metabolism ; Solubility ; Ubiquitin-Conjugating Enzymes/genetics/metabolism ; Ubiquitination ; Von Hippel-Lindau Tumor Suppressor Protein/chemistry/genetics/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)
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  • 2
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    Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-07
    Description: Molecular chaperones in the eukaryotic cytosol were shown to interact differently with chemically denatured proteins and their newly translated counterparts. During refolding from denaturant, actin partitioned freely between 70-kilodalton heat shock protein, the bulk cytosol, and the chaperonin TCP1-ring complex. In contrast, during cell-free translation, the chaperones were recruited to the elongating polypeptide and protected it from exposure to the bulk cytosol during folding. Posttranslational cycling between chaperone-bound and free states was observed with subunits of oligomeric proteins and with aberrant polypeptides; this cycling allowed the subunits to assemble and the aberrant polypeptides to be degraded. Thus, folding, oligomerization, and degradation are linked hierarchically to ensure the correct fate of newly synthesized polypeptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frydman, J -- Hartl, F U -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1497-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633246" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*chemistry/genetics/metabolism ; Adenosine Triphosphate/metabolism ; Cell Extracts ; Chaperonin 60/chemistry/metabolism ; Chaperonin Containing TCP-1 ; Chaperonins/chemistry/metabolism ; HSP70 Heat-Shock Proteins/chemistry/metabolism ; Luciferases/*chemistry/genetics/metabolism ; Molecular Chaperones/chemistry/*metabolism ; Peptides/chemistry/metabolism ; *Protein Biosynthesis ; Protein Conformation ; Protein Denaturation ; *Protein Folding ; Reticulocytes ; Ribosomes/metabolism
    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)
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