Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking
Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported...
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| Veröffentlicht in: | Scientific reports 2016-06, Vol.6 (1), p.26965-26965, Article 26965 |
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| creator | Butkevich, Eugenia Härtig, Wolfgang Nikolov, Miroslav Erck, Christian Grosche, Jens Urlaub, Henning Schmidt, Christoph F. Klopfenstein, Dieter R. Chua, John Jia En |
| description | Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer’s disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration. |
| doi_str_mv | 10.1038/srep26965 |
| format | Article |
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The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer’s disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep26965</identifier><identifier>PMID: 27247180</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/1 ; 13/106 ; 13/109 ; 13/44 ; 13/51 ; 14/34 ; 14/35 ; 38 ; 42 ; 631/378/340 ; 631/378/87 ; 631/80/128/1923 ; 631/80/2023/2022 ; 631/80/458/1733 ; 64/11 ; 64/110 ; 82/29 ; 82/58 ; Alzheimer's disease ; Animals ; Animals, Genetically Modified ; Axonal Transport - genetics ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins - genetics ; Cerebral Cortex - metabolism ; Cerebral Cortex - pathology ; Gene Expression Regulation ; HEK293 Cells ; HeLa Cells ; Hippocampus - metabolism ; Hippocampus - pathology ; Humanities and Social Sciences ; Humans ; Kinases ; Kinesin - genetics ; Mice ; multidisciplinary ; Mutation ; Neurons - metabolism ; Neurons - pathology ; Peptides ; Phosphorylation ; Protein-Serine-Threonine Kinases - deficiency ; Protein-Serine-Threonine Kinases - genetics ; Proteins ; Rats ; Science ; Science (multidisciplinary) ; Synaptic Transmission ; Synaptic Vesicles - metabolism ; Synaptic Vesicles - pathology ; Tumor Suppressor Proteins - deficiency ; Tumor Suppressor Proteins - genetics</subject><ispartof>Scientific reports, 2016-06, Vol.6 (1), p.26965-26965, Article 26965</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group Jun 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-bc897e2e64e8f1f50d4672371adb3ce6c9ce55d5225d20fce9ccd6675d694e543</citedby><cites>FETCH-LOGICAL-c504t-bc897e2e64e8f1f50d4672371adb3ce6c9ce55d5225d20fce9ccd6675d694e543</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/PMC4887895/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4887895/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27922,27923,41118,42187,51574,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27247180$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Butkevich, Eugenia</creatorcontrib><creatorcontrib>Härtig, Wolfgang</creatorcontrib><creatorcontrib>Nikolov, Miroslav</creatorcontrib><creatorcontrib>Erck, Christian</creatorcontrib><creatorcontrib>Grosche, Jens</creatorcontrib><creatorcontrib>Urlaub, Henning</creatorcontrib><creatorcontrib>Schmidt, Christoph F.</creatorcontrib><creatorcontrib>Klopfenstein, Dieter R.</creatorcontrib><creatorcontrib>Chua, John Jia En</creatorcontrib><title>Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer’s disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration.</description><subject>13/1</subject><subject>13/106</subject><subject>13/109</subject><subject>13/44</subject><subject>13/51</subject><subject>14/34</subject><subject>14/35</subject><subject>38</subject><subject>42</subject><subject>631/378/340</subject><subject>631/378/87</subject><subject>631/80/128/1923</subject><subject>631/80/2023/2022</subject><subject>631/80/458/1733</subject><subject>64/11</subject><subject>64/110</subject><subject>82/29</subject><subject>82/58</subject><subject>Alzheimer's disease</subject><subject>Animals</subject><subject>Animals, Genetically Modified</subject><subject>Axonal Transport - genetics</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Cerebral Cortex - metabolism</subject><subject>Cerebral Cortex - pathology</subject><subject>Gene Expression Regulation</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Hippocampus - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Butkevich, Eugenia</au><au>Härtig, Wolfgang</au><au>Nikolov, Miroslav</au><au>Erck, Christian</au><au>Grosche, Jens</au><au>Urlaub, Henning</au><au>Schmidt, Christoph F.</au><au>Klopfenstein, Dieter R.</au><au>Chua, John Jia En</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2016-06-01</date><risdate>2016</risdate><volume>6</volume><issue>1</issue><spage>26965</spage><epage>26965</epage><pages>26965-26965</pages><artnum>26965</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Adapters bind motor proteins to cargoes and therefore play essential roles in Kinesin-1 mediated intracellular transport. The regulatory mechanisms governing adapter functions and the spectrum of cargoes recognized by individual adapters remain poorly defined. Here, we show that cargoes transported by the Kinesin-1 adapter FEZ1 are enriched for presynaptic components and identify that specific phosphorylation of FEZ1 at its serine 58 regulatory site is mediated by microtubule affinity-regulating kinases (MARK/PAR-1). Loss of MARK/PAR-1 impairs axonal transport, with adapter and cargo abnormally co-aggregating in neuronal cell bodies and axons. Presynaptic specializations are markedly reduced and distorted in FEZ1 and MARK/PAR-1 mutants. Strikingly, abnormal co-aggregates of unphosphorylated FEZ1, Kinesin-1 and its putative cargoes are present in brains of transgenic mice modelling aspects of Alzheimer’s disease, a neurodegenerative disorder exhibiting impaired axonal transport and altered MARK activity. Our findings suggest that perturbed FEZ1-mediated synaptic delivery of proteins arising from abnormal signalling potentially contributes to the process of neurodegeneration.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27247180</pmid><doi>10.1038/srep26965</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 13/1 13/106 13/109 13/44 13/51 14/34 14/35 38 42 631/378/340 631/378/87 631/80/128/1923 631/80/2023/2022 631/80/458/1733 64/11 64/110 82/29 82/58 Alzheimer's disease Animals Animals, Genetically Modified Axonal Transport - genetics Caenorhabditis elegans Caenorhabditis elegans Proteins - genetics Cerebral Cortex - metabolism Cerebral Cortex - pathology Gene Expression Regulation HEK293 Cells HeLa Cells Hippocampus - metabolism Hippocampus - pathology Humanities and Social Sciences Humans Kinases Kinesin - genetics Mice multidisciplinary Mutation Neurons - metabolism Neurons - pathology Peptides Phosphorylation Protein-Serine-Threonine Kinases - deficiency Protein-Serine-Threonine Kinases - genetics Proteins Rats Science Science (multidisciplinary) Synaptic Transmission Synaptic Vesicles - metabolism Synaptic Vesicles - pathology Tumor Suppressor Proteins - deficiency Tumor Suppressor Proteins - genetics |
| title | Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking |
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