Loading…
Cellular factors modulating the mechanism of tau protein aggregation
Pathological accumulation of the microtubule-associated protein tau, in the form of neurofibrillary tangles, is a major hallmark of Alzheimer’s disease, the most prevalent neurodegenerative condition worldwide. In addition to Alzheimer’s disease, a number of neurodegenerative diseases, called tauopa...
Saved in:
Published in: | Cellular and Molecular Life Sciences 2015-05, Vol.72 (10), p.1863-1879 |
---|---|
Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993 |
---|---|
cites | cdi_FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993 |
container_end_page | 1879 |
container_issue | 10 |
container_start_page | 1863 |
container_title | Cellular and Molecular Life Sciences |
container_volume | 72 |
creator | Fontaine, Sarah N Sabbagh, Jonathan J Baker, Jeremy Martinez-Licha, Carlos R Darling, April Dickey, Chad A |
description | Pathological accumulation of the microtubule-associated protein tau, in the form of neurofibrillary tangles, is a major hallmark of Alzheimer’s disease, the most prevalent neurodegenerative condition worldwide. In addition to Alzheimer’s disease, a number of neurodegenerative diseases, called tauopathies, are characterized by the accumulation of aggregated tau in a variety of brain regions. While tau normally plays an important role in stabilizing the microtubule network of the cytoskeleton, its dissociation from microtubules and eventual aggregation into pathological deposits is an area of intense focus for therapeutic development. Here we discuss the known cellular factors that affect tau aggregation, from post-translational modifications to molecular chaperones. |
doi_str_mv | 10.1007/s00018-015-1839-9 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4406819</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3660280541</sourcerecordid><originalsourceid>FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993</originalsourceid><addsrcrecordid>eNp9kU1v1DAQhq0K1JbSH9ALROqFS8B2Ese-IFXLp1SJQ1uJmzWxx9lUib3YSSX-PV6yVIUDvtjWPPPOx0vIBaNvGaXtu0QpZbKkrCmZrFSpjsgpqzktFW3Zs8NbSP79hLxI6T7DjeTimJzwRggh2_aUfNjgOC4jxMKBmUNMxRRs_s-D74t5i8WEZgt-SFMRXDHDUuximHHwBfR9xD6Dwb8kzx2MCc8P9xm5-_TxdvOlvP72-evm6ro0jaBzCdbVDhrrqrqjYJpOWDQ1AoVOtthiYznnrXNIGWKNorNWOmBCWuM4U6o6I-9X3d3STWgN-jnCqHdxmCD-1AEG_XfED1vdhwdd11RIthd4cxCI4ceCadbTkEzeAHgMS9JMtLUSebdVRi__Qe_DEn0e7zeVD1cyU2ylTAwpRXSPzTCq9x7p1SOdV6_3Hul9E6-eTvGY8ceUDPAVSDnke4xPSv9H9fWa5CBo6OOQ9N0Np0xkkiuqePULR8-oIg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1674444298</pqid></control><display><type>article</type><title>Cellular factors modulating the mechanism of tau protein aggregation</title><source>Springer Link</source><source>PubMed Central</source><creator>Fontaine, Sarah N ; Sabbagh, Jonathan J ; Baker, Jeremy ; Martinez-Licha, Carlos R ; Darling, April ; Dickey, Chad A</creator><creatorcontrib>Fontaine, Sarah N ; Sabbagh, Jonathan J ; Baker, Jeremy ; Martinez-Licha, Carlos R ; Darling, April ; Dickey, Chad A</creatorcontrib><description>Pathological accumulation of the microtubule-associated protein tau, in the form of neurofibrillary tangles, is a major hallmark of Alzheimer’s disease, the most prevalent neurodegenerative condition worldwide. In addition to Alzheimer’s disease, a number of neurodegenerative diseases, called tauopathies, are characterized by the accumulation of aggregated tau in a variety of brain regions. While tau normally plays an important role in stabilizing the microtubule network of the cytoskeleton, its dissociation from microtubules and eventual aggregation into pathological deposits is an area of intense focus for therapeutic development. Here we discuss the known cellular factors that affect tau aggregation, from post-translational modifications to molecular chaperones.</description><identifier>ISSN: 1420-682X</identifier><identifier>EISSN: 1420-9071</identifier><identifier>DOI: 10.1007/s00018-015-1839-9</identifier><identifier>PMID: 25666877</identifier><language>eng</language><publisher>Basel: Springer-Verlag</publisher><subject>Acetylation ; Alzheimer disease ; Alzheimer Disease - physiopathology ; Alzheimer's disease ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; brain ; Cell Biology ; dissociation ; Glycosylation ; Heat-Shock Proteins - metabolism ; Humans ; Life Sciences ; microtubules ; Microtubules - metabolism ; molecular chaperones ; Molecular Chaperones - metabolism ; Neurodegeneration ; neurodegenerative diseases ; Pathology ; Phosphorylation ; post-translational modification ; Protein Aggregation, Pathological - metabolism ; Proteins ; Proteolysis ; Review ; tau Proteins - genetics ; tau Proteins - metabolism</subject><ispartof>Cellular and Molecular Life Sciences, 2015-05, Vol.72 (10), p.1863-1879</ispartof><rights>Springer Basel 2015</rights><rights>Springer Basel 2015 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993</citedby><cites>FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4406819/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4406819/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,315,733,786,790,798,891,27955,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25666877$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fontaine, Sarah N</creatorcontrib><creatorcontrib>Sabbagh, Jonathan J</creatorcontrib><creatorcontrib>Baker, Jeremy</creatorcontrib><creatorcontrib>Martinez-Licha, Carlos R</creatorcontrib><creatorcontrib>Darling, April</creatorcontrib><creatorcontrib>Dickey, Chad A</creatorcontrib><title>Cellular factors modulating the mechanism of tau protein aggregation</title><title>Cellular and Molecular Life Sciences</title><addtitle>Cell. Mol. Life Sci</addtitle><addtitle>Cell Mol Life Sci</addtitle><description>Pathological accumulation of the microtubule-associated protein tau, in the form of neurofibrillary tangles, is a major hallmark of Alzheimer’s disease, the most prevalent neurodegenerative condition worldwide. In addition to Alzheimer’s disease, a number of neurodegenerative diseases, called tauopathies, are characterized by the accumulation of aggregated tau in a variety of brain regions. While tau normally plays an important role in stabilizing the microtubule network of the cytoskeleton, its dissociation from microtubules and eventual aggregation into pathological deposits is an area of intense focus for therapeutic development. Here we discuss the known cellular factors that affect tau aggregation, from post-translational modifications to molecular chaperones.</description><subject>Acetylation</subject><subject>Alzheimer disease</subject><subject>Alzheimer Disease - physiopathology</subject><subject>Alzheimer's disease</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>brain</subject><subject>Cell Biology</subject><subject>dissociation</subject><subject>Glycosylation</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>microtubules</subject><subject>Microtubules - metabolism</subject><subject>molecular chaperones</subject><subject>Molecular Chaperones - metabolism</subject><subject>Neurodegeneration</subject><subject>neurodegenerative diseases</subject><subject>Pathology</subject><subject>Phosphorylation</subject><subject>post-translational modification</subject><subject>Protein Aggregation, Pathological - metabolism</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Review</subject><subject>tau Proteins - genetics</subject><subject>tau Proteins - metabolism</subject><issn>1420-682X</issn><issn>1420-9071</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNp9kU1v1DAQhq0K1JbSH9ALROqFS8B2Ese-IFXLp1SJQ1uJmzWxx9lUib3YSSX-PV6yVIUDvtjWPPPOx0vIBaNvGaXtu0QpZbKkrCmZrFSpjsgpqzktFW3Zs8NbSP79hLxI6T7DjeTimJzwRggh2_aUfNjgOC4jxMKBmUNMxRRs_s-D74t5i8WEZgt-SFMRXDHDUuximHHwBfR9xD6Dwb8kzx2MCc8P9xm5-_TxdvOlvP72-evm6ro0jaBzCdbVDhrrqrqjYJpOWDQ1AoVOtthiYznnrXNIGWKNorNWOmBCWuM4U6o6I-9X3d3STWgN-jnCqHdxmCD-1AEG_XfED1vdhwdd11RIthd4cxCI4ceCadbTkEzeAHgMS9JMtLUSebdVRi__Qe_DEn0e7zeVD1cyU2ylTAwpRXSPzTCq9x7p1SOdV6_3Hul9E6-eTvGY8ceUDPAVSDnke4xPSv9H9fWa5CBo6OOQ9N0Np0xkkiuqePULR8-oIg</recordid><startdate>20150501</startdate><enddate>20150501</enddate><creator>Fontaine, Sarah N</creator><creator>Sabbagh, Jonathan J</creator><creator>Baker, Jeremy</creator><creator>Martinez-Licha, Carlos R</creator><creator>Darling, April</creator><creator>Dickey, Chad A</creator><general>Springer-Verlag</general><general>Springer Basel</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PATMY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150501</creationdate><title>Cellular factors modulating the mechanism of tau protein aggregation</title><author>Fontaine, Sarah N ; Sabbagh, Jonathan J ; Baker, Jeremy ; Martinez-Licha, Carlos R ; Darling, April ; Dickey, Chad A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Acetylation</topic><topic>Alzheimer disease</topic><topic>Alzheimer Disease - physiopathology</topic><topic>Alzheimer's disease</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>brain</topic><topic>Cell Biology</topic><topic>dissociation</topic><topic>Glycosylation</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>microtubules</topic><topic>Microtubules - metabolism</topic><topic>molecular chaperones</topic><topic>Molecular Chaperones - metabolism</topic><topic>Neurodegeneration</topic><topic>neurodegenerative diseases</topic><topic>Pathology</topic><topic>Phosphorylation</topic><topic>post-translational modification</topic><topic>Protein Aggregation, Pathological - metabolism</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Review</topic><topic>tau Proteins - genetics</topic><topic>tau Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fontaine, Sarah N</creatorcontrib><creatorcontrib>Sabbagh, Jonathan J</creatorcontrib><creatorcontrib>Baker, Jeremy</creatorcontrib><creatorcontrib>Martinez-Licha, Carlos R</creatorcontrib><creatorcontrib>Darling, April</creatorcontrib><creatorcontrib>Dickey, Chad A</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Research Library (ProQuest)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cellular and Molecular Life Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fontaine, Sarah N</au><au>Sabbagh, Jonathan J</au><au>Baker, Jeremy</au><au>Martinez-Licha, Carlos R</au><au>Darling, April</au><au>Dickey, Chad A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cellular factors modulating the mechanism of tau protein aggregation</atitle><jtitle>Cellular and Molecular Life Sciences</jtitle><stitle>Cell. Mol. Life Sci</stitle><addtitle>Cell Mol Life Sci</addtitle><date>2015-05-01</date><risdate>2015</risdate><volume>72</volume><issue>10</issue><spage>1863</spage><epage>1879</epage><pages>1863-1879</pages><issn>1420-682X</issn><eissn>1420-9071</eissn><notes>http://dx.doi.org/10.1007/s00018-015-1839-9</notes><notes>ObjectType-Article-2</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-3</notes><notes>content type line 23</notes><notes>ObjectType-Review-1</notes><abstract>Pathological accumulation of the microtubule-associated protein tau, in the form of neurofibrillary tangles, is a major hallmark of Alzheimer’s disease, the most prevalent neurodegenerative condition worldwide. In addition to Alzheimer’s disease, a number of neurodegenerative diseases, called tauopathies, are characterized by the accumulation of aggregated tau in a variety of brain regions. While tau normally plays an important role in stabilizing the microtubule network of the cytoskeleton, its dissociation from microtubules and eventual aggregation into pathological deposits is an area of intense focus for therapeutic development. Here we discuss the known cellular factors that affect tau aggregation, from post-translational modifications to molecular chaperones.</abstract><cop>Basel</cop><pub>Springer-Verlag</pub><pmid>25666877</pmid><doi>10.1007/s00018-015-1839-9</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1420-682X |
ispartof | Cellular and Molecular Life Sciences, 2015-05, Vol.72 (10), p.1863-1879 |
issn | 1420-682X 1420-9071 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4406819 |
source | Springer Link; PubMed Central |
subjects | Acetylation Alzheimer disease Alzheimer Disease - physiopathology Alzheimer's disease Biochemistry Biomedical and Life Sciences Biomedicine brain Cell Biology dissociation Glycosylation Heat-Shock Proteins - metabolism Humans Life Sciences microtubules Microtubules - metabolism molecular chaperones Molecular Chaperones - metabolism Neurodegeneration neurodegenerative diseases Pathology Phosphorylation post-translational modification Protein Aggregation, Pathological - metabolism Proteins Proteolysis Review tau Proteins - genetics tau Proteins - metabolism |
title | Cellular factors modulating the mechanism of tau protein aggregation |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-21T12%3A42%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cellular%20factors%20modulating%20the%20mechanism%20of%20tau%20protein%20aggregation&rft.jtitle=Cellular%20and%20Molecular%20Life%20Sciences&rft.au=Fontaine,%20Sarah%20N&rft.date=2015-05-01&rft.volume=72&rft.issue=10&rft.spage=1863&rft.epage=1879&rft.pages=1863-1879&rft.issn=1420-682X&rft.eissn=1420-9071&rft_id=info:doi/10.1007/s00018-015-1839-9&rft_dat=%3Cproquest_pubme%3E3660280541%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c560t-adf4fa5df34b0ac5b6dec4ea0ab87e7e5d2227ffe01ee4e6bdd8fa168dcf21993%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1674444298&rft_id=info:pmid/25666877&rfr_iscdi=true |