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  • 1
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    Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-17
    Description: The 26S proteasome mediates degradation of ubiquitin-conjugated proteins. Although ubiquitin is recycled from proteasome substrates, the molecular basis of deubiquitination at the proteasome and its relation to substrate degradation remain unknown. The Rpn11 subunit of the proteasome lid subcomplex contains a highly conserved Jab1/MPN domain-associated metalloisopeptidase (JAMM) motif-EX(n)HXHX(10)D. Mutation of the predicted active-site histidines to alanine (rpn11AXA) was lethal and stabilized ubiquitin pathway substrates in yeast. Rpn11(AXA) mutant proteasomes assembled normally but failed to either deubiquitinate or degrade ubiquitinated Sic1 in vitro. Our findings reveal an unexpected coupling between substrate deubiquitination and degradation and suggest a unifying rationale for the presence of the lid in eukaryotic proteasomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, Rati -- Aravind, L -- Oania, Robert -- McDonald, W Hayes -- Yates, John R 3rd -- Koonin, Eugene V -- Deshaies, Raymond J -- RR11823-05-01/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 18;298(5593):611-5. Epub 2002 Aug 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12183636" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Binding Sites ; Carbon-Nitrogen Lyases/chemistry/*metabolism ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cysteine Endopeptidases/metabolism ; DNA-Binding Proteins/chemistry ; Endopeptidases/chemistry/*metabolism ; Fungal Proteins/*metabolism ; Metalloendopeptidases/chemistry/*metabolism ; Molecular Sequence Data ; Multienzyme Complexes/metabolism ; Mutation ; Oligopeptides/pharmacology ; Peptide Hydrolases/*metabolism ; Proteasome Endopeptidase Complex ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Transcription Factors/chemistry ; Ubiquitins/*metabolism ; Yeasts/metabolism ; Zinc/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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    Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-12-19
    Description: Palmitoylation regulates diverse aspects of neuronal protein trafficking and function. Here a global characterization of rat neural palmitoyl-proteomes identifies most of the known neural palmitoyl proteins-68 in total, plus more than 200 new palmitoyl-protein candidates, with further testing confirming palmitoylation for 21 of these candidates. The new palmitoyl proteins include neurotransmitter receptors, transporters, adhesion molecules, scaffolding proteins, as well as SNAREs and other vesicular trafficking proteins. Of particular interest is the finding of palmitoylation for a brain-specific Cdc42 splice variant. The palmitoylated Cdc42 isoform (Cdc42-palm) differs from the canonical, prenylated form (Cdc42-prenyl), both with regard to localization and function: Cdc42-palm concentrates in dendritic spines and has a special role in inducing these post-synaptic structures. Furthermore, assessing palmitoylation dynamics in drug-induced activity models identifies rapidly induced changes for Cdc42 as well as for other synaptic palmitoyl proteins, suggesting that palmitoylation may participate broadly in the activity-driven changes that shape synapse morphology and function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2610860/" 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/PMC2610860/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, Rujun -- Wan, Junmei -- Arstikaitis, Pamela -- Takahashi, Hideto -- Huang, Kun -- Bailey, Aaron O -- Thompson, James X -- Roth, Amy F -- Drisdel, Renaldo C -- Mastro, Ryan -- Green, William N -- Yates, John R 3rd -- Davis, Nicholas G -- El-Husseini, Alaa -- DA019695/DA/NIDA NIH HHS/ -- DA13602/DA/NIDA NIH HHS/ -- GM65525/GM/NIGMS NIH HHS/ -- NS043782/NS/NINDS NIH HHS/ -- P01 DA019695/DA/NIDA NIH HHS/ -- P01 DA019695-01A20001/DA/NIDA NIH HHS/ -- P01 DA019695-020001/DA/NIDA NIH HHS/ -- R01 DA013602/DA/NIDA NIH HHS/ -- R01 DA013602-01/DA/NIDA NIH HHS/ -- R01 DA013602-02/DA/NIDA NIH HHS/ -- R01 DA013602-02S1/DA/NIDA NIH HHS/ -- R01 DA013602-02S2/DA/NIDA NIH HHS/ -- R01 DA013602-03/DA/NIDA NIH HHS/ -- R01 DA013602-04/DA/NIDA NIH HHS/ -- R01 DA013602-05/DA/NIDA NIH HHS/ -- R01 NS032693/NS/NINDS NIH HHS/ -- R01 NS032693-08/NS/NINDS NIH HHS/ -- R01 NS043782/NS/NINDS NIH HHS/ -- R01 NS043782-01A2/NS/NINDS NIH HHS/ -- R01 NS043782-02/NS/NINDS NIH HHS/ -- R01 NS043782-03/NS/NINDS NIH HHS/ -- R01 NS043782-04/NS/NINDS NIH HHS/ -- R01 NS043782-05/NS/NINDS NIH HHS/ -- R56 NS043782/NS/NINDS NIH HHS/ -- R56 NS043782-06/NS/NINDS NIH HHS/ -- RR011823/RR/NCRR NIH HHS/ -- England -- Nature. 2008 Dec 18;456(7224):904-9. doi: 10.1038/nature07605.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, Brain Research Centre, University of British Columbia, Vancouver V6T 1Z3, British Columbia, Canada. rkang@interchange.ubc.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19092927" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing/genetics ; Animals ; Cells, Cultured ; Cerebral Cortex/cytology/embryology ; Dendrites/metabolism ; *Lipoylation ; Models, Neurological ; Neurons/*metabolism ; Organ Specificity ; Proteome/metabolism ; *Proteomics ; Rats ; Synapses/*metabolism ; cdc42 GTP-Binding Protein/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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  • 3
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    A cell cycle phosphoproteome of the yeast centrosome (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-06-28
    Description: Centrosomes organize the bipolar mitotic spindle, and centrosomal defects cause chromosome instability. Protein phosphorylation modulates centrosome function, and we provide a comprehensive map of phosphorylation on intact yeast centrosomes (18 proteins). Mass spectrometry was used to identify 297 phosphorylation sites on centrosomes from different cell cycle stages. We observed different modes of phosphoregulation via specific protein kinases, phosphorylation site clustering, and conserved phosphorylated residues. Mutating all eight cyclin-dependent kinase (Cdk)-directed sites within the core component, Spc42, resulted in lethality and reduced centrosomal assembly. Alternatively, mutation of one conserved Cdk site within gamma-tubulin (Tub4-S360D) caused mitotic delay and aberrant anaphase spindle elongation. Our work establishes the extent and complexity of this prominent posttranslational modification in centrosome biology and provides specific examples of phosphorylation control in centrosome function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3825980/" 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/PMC3825980/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keck, Jamie M -- Jones, Michele H -- Wong, Catherine C L -- Binkley, Jonathan -- Chen, Daici -- Jaspersen, Sue L -- Holinger, Eric P -- Xu, Tao -- Niepel, Mario -- Rout, Michael P -- Vogel, Jackie -- Sidow, Arend -- Yates, John R 3rd -- Winey, Mark -- F32 GM086038/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- MOP-64404/Canadian Institutes of Health Research/Canada -- P41 RR011823/RR/NCRR NIH HHS/ -- R01 GM051312/GM/NIGMS NIH HHS/ -- R01 GM051312-16/GM/NIGMS NIH HHS/ -- R01 GM051312-16S1/GM/NIGMS NIH HHS/ -- R01 GM062427/GM/NIGMS NIH HHS/ -- R01 HG003039/HG/NHGRI NIH HHS/ -- T32 GM008759/GM/NIGMS NIH HHS/ -- U54 RR022220/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2011 Jun 24;332(6037):1557-61. doi: 10.1126/science.1205193.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21700874" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; CDC2 Protein Kinase/metabolism ; *Cell Cycle ; Centrosome/*metabolism/ultrastructure ; Cytoskeletal Proteins/genetics/metabolism ; Fungal Proteins/chemistry/metabolism ; Fungi/metabolism ; G1 Phase ; Mitosis ; Mutation ; Phosphoproteins/genetics/metabolism ; Phosphorylation ; Protein Processing, Post-Translational ; Proteome/*metabolism ; Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Spindle Apparatus/metabolism/ultrastructure ; Tubulin/chemistry/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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  • 4
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    Extremely long-lived nuclear pore proteins in the rat brain (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-02-04
    Description: To combat the functional decline of the proteome, cells use the process of protein turnover to replace potentially impaired polypeptides with new functional copies. We found that extremely long-lived proteins (ELLPs) did not turn over in postmitotic cells of the rat central nervous system. These ELLPs were associated with chromatin and the nuclear pore complex, the central transport channels that mediate all molecular trafficking in and out of the nucleus. The longevity of these proteins would be expected to expose them to potentially harmful metabolites, putting them at risk of accumulating damage over extended periods of time. Thus, it is possible that failure to maintain proper levels and functional integrity of ELLPs in nonproliferative cells might contribute to age-related deterioration in cell and tissue function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296478/" 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/PMC3296478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Savas, Jeffrey N -- Toyama, Brandon H -- Xu, Tao -- Yates, John R 3rd -- Hetzer, Martin W -- F32 AG039127/AG/NIA NIH HHS/ -- F32 AG039127-01A1/AG/NIA NIH HHS/ -- F32AG039127/AG/NIA NIH HHS/ -- HHSN268201000035C/PHS HHS/ -- P01 AG031097/AG/NIA NIH HHS/ -- P01 AG031097-03/AG/NIA NIH HHS/ -- P30 CA014195/CA/NCI NIH HHS/ -- P30 CA014195-35/CA/NCI NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- P41 RR011823-14/RR/NCRR NIH HHS/ -- R01 MH067880/MH/NIMH NIH HHS/ -- R01 MH067880-08/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2012 Feb 24;335(6071):942. doi: 10.1126/science.1217421. Epub 2012 Feb 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22300851" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/*metabolism ; Cell Aging ; Chromatin/metabolism ; Female ; Half-Life ; Liver/metabolism ; Mitosis ; Nuclear Pore/*metabolism ; Nuclear Pore Complex Proteins/*metabolism ; Proteome/metabolism ; Rats ; Rats, Sprague-Dawley ; Time Factors
    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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  • 5
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    Activation of the yeast Hippo pathway by phosphorylation-dependent assembly of signaling complexes (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-04-13
    Description: Scaffold-assisted signaling cascades guide cellular decision-making. In budding yeast, one such signal transduction pathway called the mitotic exit network (MEN) governs the transition from mitosis to the G1 phase of the cell cycle. The MEN is conserved and in metazoans is known as the Hippo tumor-suppressor pathway. We found that signaling through the MEN kinase cascade was mediated by an unusual two-step process. The MEN kinase Cdc15 first phosphorylated the scaffold Nud1. This created a phospho-docking site on Nud1, to which the effector kinase complex Dbf2-Mob1 bound through a phosphoserine-threonine binding domain, in order to be activated by Cdc15. This mechanism of pathway activation has implications for signal transmission through other kinase cascades and might represent a general principle in scaffold-assisted signaling.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3884217/" 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/PMC3884217/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rock, Jeremy M -- Lim, Daniel -- Stach, Lasse -- Ogrodowicz, Roksana W -- Keck, Jamie M -- Jones, Michele H -- Wong, Catherine C L -- Yates, John R 3rd -- Winey, Mark -- Smerdon, Stephen J -- Yaffe, Michael B -- Amon, Angelika -- CA112967/CA/NCI NIH HHS/ -- ES015339/ES/NIEHS NIH HHS/ -- F32 GM086038/GM/NIGMS NIH HHS/ -- GM056800/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- MC_U117584228/Medical Research Council/United Kingdom -- P30 CA014051/CA/NCI NIH HHS/ -- P41 GM103533/GM/NIGMS NIH HHS/ -- P41 RR011823/RR/NCRR NIH HHS/ -- R01 ES015339/ES/NIEHS NIH HHS/ -- R01 GM051312/GM/NIGMS NIH HHS/ -- R01 GM056800/GM/NIGMS NIH HHS/ -- R29 GM056800/GM/NIGMS NIH HHS/ -- U117584228/Medical Research Council/United Kingdom -- U54 CA112967/CA/NCI NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2013 May 17;340(6134):871-5. doi: 10.1126/science.1235822. Epub 2013 Apr 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23579499" target="_blank"〉PubMed〈/a〉
    Keywords: Anaphase ; Cell Cycle Proteins/chemistry/*metabolism ; Deoxyribonucleases/chemistry/*metabolism ; Enzyme Activation ; GTP-Binding Proteins/*metabolism ; *Mitosis ; Phosphoproteins/chemistry/*metabolism ; Phosphorylation ; Protein Conformation ; Protein-Serine-Threonine Kinases/*metabolism ; Saccharomyces cerevisiae/cytology/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Signal Transduction ; tRNA Methyltransferases/chemistry/*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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  • 6
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    HSF-1-mediated cytoskeletal integrity determines thermotolerance and life span (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-10-18
    Description: The conserved heat shock transcription factor-1 (HSF-1) is essential to cellular stress resistance and life-span determination. The canonical function of HSF-1 is to regulate a network of genes encoding molecular chaperones that protect proteins from damage caused by extrinsic environmental stress or intrinsic age-related deterioration. In Caenorhabditis elegans, we engineered a modified HSF-1 strain that increased stress resistance and longevity without enhanced chaperone induction. This health assurance acted through the regulation of the calcium-binding protein PAT-10. Loss of pat-10 caused a collapse of the actin cytoskeleton, stress resistance, and life span. Furthermore, overexpression of pat-10 increased actin filament stability, thermotolerance, and longevity, indicating that in addition to chaperone regulation, HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4403873/" 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/PMC4403873/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baird, Nathan A -- Douglas, Peter M -- Simic, Milos S -- Grant, Ana R -- Moresco, James J -- Wolff, Suzanne C -- Yates, John R 3rd -- Manning, Gerard -- Dillin, Andrew -- 1K99AG042495-01A1/AG/NIA NIH HHS/ -- 5P41RR011823-17/RR/NCRR NIH HHS/ -- 8 P41 GM103533-17/GM/NIGMS NIH HHS/ -- P01 AG031097/AG/NIA NIH HHS/ -- P40 OD010440/OD/NIH HHS/ -- P41 GM103533/GM/NIGMS NIH HHS/ -- R01AG027463-04/AG/NIA NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2014 Oct 17;346(6207):360-3. doi: 10.1126/science.1253168.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California Berkeley, Berkeley, CA 94720, USA. ; Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, MI 48109, USA. ; Scripps Research Institute, La Jolla, CA 92037, USA. ; Genentech, South San Francisco, CA 94080, USA. ; Howard Hughes Medical Institute, University of California Berkeley, Berkeley, CA 94720, USA. dillin@berkeley.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25324391" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Caenorhabditis elegans Proteins/genetics/*pharmacology/*physiology ; Cytoskeleton/*physiology/ultrastructure ; Heat-Shock Response/genetics/*physiology ; Hot Temperature ; *Longevity ; RNA Interference ; Transcription Factors/genetics/*physiology ; Troponin C/genetics/*pharmacology
    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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  • 7
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    Nuclear membrane proteins with potential disease links found by subtractive proteomics (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-06
    Description: To comprehensively identify integral membrane proteins of the nuclear envelope (NE), we prepared separately NEs and organelles known to cofractionate with them from liver. Proteins detected by multidimensional protein identification technology in the cofractionating organelles were subtracted from the NE data set. In addition to all 13 known NE integral proteins, 67 uncharacterized open reading frames with predicted membrane-spanning regions were identified. All of the eight proteins tested targeted to the NE, indicating that there are substantially more integral proteins of the NE than previously thought. Furthermore, 23 of these mapped within chromosome regions linked to a variety of dystrophies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schirmer, Eric C -- Florens, Laurence -- Guan, Tinglu -- Yates, John R 3rd -- Gerace, Larry -- F32 GM19085/GM/NIGMS NIH HHS/ -- GM28521/GM/NIGMS NIH HHS/ -- RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1380-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958361" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Cell Fractionation ; Chromosome Mapping ; DNA, Complementary ; Genetic Diseases, Inborn/*genetics ; Genetic Linkage ; Humans ; Liver/chemistry/ultrastructure ; Membrane Proteins/*analysis/genetics/isolation & purification ; Mice ; Mice, Inbred Strains ; Nuclear Envelope/*chemistry ; Nuclear Proteins/*analysis/genetics/isolation & purification ; Open Reading Frames ; Protein Structure, Tertiary ; *Proteomics ; Rats ; Rats, Sprague-Dawley
    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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  • 8
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    Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-06
    Description: Phosphorylation of the human histone variant H2A.X and H2Av, its homolog in Drosophila melanogaster, occurs rapidly at sites of DNA double-strand breaks. Little is known about the function of this phosphorylation or its removal during DNA repair. Here, we demonstrate that the Drosophila Tip60 (dTip60) chromatin-remodeling complex acetylates nucleosomal phospho-H2Av and exchanges it with an unmodified H2Av. Both the histone acetyltransferase dTip60 as well as the adenosine triphosphatase Domino/p400 catalyze the exchange of phospho-H2Av. Thus, these data reveal a previously unknown mechanism for selective histone exchange that uses the concerted action of two distinct chromatin-remodeling enzymes within the same multiprotein complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kusch, Thomas -- Florens, Laurence -- Macdonald, W Hayes -- Swanson, Selene K -- Glaser, Robert L -- Yates, John R 3rd -- Abmayr, Susan M -- Washburn, Michael P -- Workman, Jerry L -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2084-7. Epub 2004 Nov 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110, USA. tnk@stowers-institute.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528408" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/genetics/*metabolism ; Adenosine Triphosphatases/metabolism ; Animals ; Cell Line ; *DNA Damage ; DNA Repair ; Dimerization ; Drosophila Proteins/genetics/metabolism ; Drosophila melanogaster/embryology/genetics/*metabolism ; Embryo, Nonmammalian/metabolism ; Histone Acetyltransferases ; Histones/*metabolism ; Multiprotein Complexes/*metabolism ; Nucleosomes/*metabolism ; Phosphorylation ; RNA Interference ; Recombinant Proteins/metabolism ; Transcription Factors/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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  • 9
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    Glial membranes at the node of Ranvier prevent neurite outgrowth (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-19
    Description: Nodes of Ranvier are regularly placed, nonmyelinated axon segments along myelinated nerves. Here we show that nodal membranes isolated from the central nervous system (CNS) of mammals restricted neurite outgrowth of cultured neurons. Proteomic analysis of these membranes revealed several inhibitors of neurite outgrowth, including the oligodendrocyte myelin glycoprotein (OMgp). In rat spinal cord, OMgp was not localized to compact myelin, as previously thought, but to oligodendroglia-like cells, whose processes converge to form a ring that completely encircles the nodes. In OMgp-null mice, CNS nodes were abnormally wide and collateral sprouting was observed. Nodal ensheathment in the CNS may stabilize the node and prevent axonal sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Jeffrey K -- Phillips, Greg R -- Roth, Alejandro D -- Pedraza, Liliana -- Shan, Weisong -- Belkaid, Wiam -- Mi, Sha -- Fex-Svenningsen, Asa -- Florens, Laurence -- Yates, John R 3rd -- Colman, David R -- NS20147/NS/NINDS NIH HHS/ -- P41 RR11823/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2005 Dec 16;310(5755):1813-7. Epub 2005 Nov 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fishberg Department of Neuroscience, Mount Sinai School of Medicine, One Gustave L. Levy Place, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16293723" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/analysis ; Axons/*physiology/ultrastructure ; Cattle ; Cell Surface Extensions/chemistry/*physiology/ultrastructure ; Cells, Cultured ; GPI-Linked Proteins ; Ganglia, Spinal/physiology/ultrastructure ; Humans ; Mice ; Myelin Proteins ; Myelin Sheath/chemistry ; Myelin-Associated Glycoprotein/analysis ; Myelin-Oligodendrocyte Glycoprotein ; Neurites/*physiology/ultrastructure ; Neuroglia/chemistry/*physiology/*ultrastructure ; Oligodendroglia/chemistry/physiology/ultrastructure ; Proteoglycans/analysis ; Proteomics ; Ranvier's Nodes/chemistry/*physiology/ultrastructure ; Rats ; Spinal Cord/cytology
    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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  • 10
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    A comprehensive survey of the Plasmodium life cycle by genomic, transcriptomic, and proteomic analyses (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-08
    Description: Plasmodium berghei and Plasmodium chabaudi are widely used model malaria species. Comparison of their genomes, integrated with proteomic and microarray data, with the genomes of Plasmodium falciparum and Plasmodium yoelii revealed a conserved core of 4500 Plasmodium genes in the central regions of the 14 chromosomes and highlighted genes evolving rapidly because of stage-specific selective pressures. Four strategies for gene expression are apparent during the parasites' life cycle: (i) housekeeping; (ii) host-related; (iii) strategy-specific related to invasion, asexual replication, and sexual development; and (iv) stage-specific. We observed posttranscriptional gene silencing through translational repression of messenger RNA during sexual development, and a 47-base 3' untranslated region motif is implicated in this process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, Neil -- Karras, Marianna -- Raine, J Dale -- Carlton, Jane M -- Kooij, Taco W A -- Berriman, Matthew -- Florens, Laurence -- Janssen, Christoph S -- Pain, Arnab -- Christophides, Georges K -- James, Keith -- Rutherford, Kim -- Harris, Barbara -- Harris, David -- Churcher, Carol -- Quail, Michael A -- Ormond, Doug -- Doggett, Jon -- Trueman, Holly E -- Mendoza, Jacqui -- Bidwell, Shelby L -- Rajandream, Marie-Adele -- Carucci, Daniel J -- Yates, John R 3rd -- Kafatos, Fotis C -- Janse, Chris J -- Barrell, Bart -- Turner, C Michael R -- Waters, Andrew P -- Sinden, Robert E -- New York, N.Y. -- Science. 2005 Jan 7;307(5706):82-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pathogen Sequencing Unit, Wellcome Trust Sanger Institute, Genome Campus, Hinxton, Cambridge CB10 1SA, UK. nhall@tigr.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15637271" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Animals ; Anopheles/parasitology ; Computational Biology ; Evolution, Molecular ; Gene Expression Profiling ; Gene Silencing ; Genes, Protozoan ; *Genome, Protozoan ; *Life Cycle Stages ; Malaria/parasitology ; Oligonucleotide Array Sequence Analysis ; Plasmodium/*genetics/*growth & development/metabolism ; Plasmodium berghei/genetics/growth & development/metabolism ; Plasmodium chabaudi/genetics/growth & development/metabolism ; Plasmodium falciparum/genetics/growth & development/metabolism ; Plasmodium yoelii/genetics/growth & development/metabolism ; Proteome/*analysis ; Proteomics ; Protozoan Proteins/analysis ; RNA, Messenger/genetics/metabolism ; RNA, Protozoan/genetics/metabolism ; Selection, Genetic ; Transcription, Genetic
    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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