Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter
Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-04, Vol.109 (15), p.5862-5867 |
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| creator | Chua, John Jia En Butkevich, Eugenia Worseck, Josephine M Kittelmann, Maike Grønborg, Mads Behrmann, Elmar Stelzl, Ulrich Pavlos, Nathan J Lalowski, Maciej M Eimer, Stefan Wanker, Erich E Klopfenstein, Dieter Robert Jahn, Reinhard |
| description | Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases. |
| doi_str_mv | 10.1073/pnas.1113819109 |
| format | Article |
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However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1113819109</identifier><identifier>PMID: 22451907</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Signal Transducing - metabolism ; Amino acids ; Animals ; Antibodies ; Axonal Transport ; Axons ; Axons - metabolism ; Binding sites ; Biological Sciences ; Caenorhabditis elegans ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins ; Caenorhabditis elegans Proteins - metabolism ; Cell membranes ; cytoplasmic streaming ; exocytosis ; Freight ; genetics ; HEK293 Cells ; Humans ; kinesin ; Kinesin - metabolism ; Kinesins ; metabolism ; molecular motor proteins ; Munc18 Proteins ; Munc18 Proteins - metabolism ; Mutant Proteins ; Mutant Proteins - metabolism ; Mutation ; Mutation - genetics ; Nematodes ; nerve tissue ; Nerve Tissue Proteins ; Nerve Tissue Proteins - metabolism ; Neurons ; Neuropeptides ; Neuropeptides - metabolism ; Neurosecretory cells ; PC12 cells ; Phosphorylation ; plasma membrane ; Protein Binding ; protein kinases ; Protein Transport ; Proteins ; serine ; synapse ; Syntaxin 1 ; Syntaxin 1 - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2012-04, Vol.109 (15), p.5862-5867</ispartof><rights>copyright © 1993-2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Apr 10, 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c622t-b3f433a11cb483201c07ce483d2e620aca4a4030318a5cf09dc3395a644c510e3</citedby><cites>FETCH-LOGICAL-c622t-b3f433a11cb483201c07ce483d2e620aca4a4030318a5cf09dc3395a644c510e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/109/15.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/41588256$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/41588256$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22451907$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chua, John Jia En</creatorcontrib><creatorcontrib>Butkevich, Eugenia</creatorcontrib><creatorcontrib>Worseck, Josephine M</creatorcontrib><creatorcontrib>Kittelmann, Maike</creatorcontrib><creatorcontrib>Grønborg, Mads</creatorcontrib><creatorcontrib>Behrmann, Elmar</creatorcontrib><creatorcontrib>Stelzl, Ulrich</creatorcontrib><creatorcontrib>Pavlos, Nathan J</creatorcontrib><creatorcontrib>Lalowski, Maciej M</creatorcontrib><creatorcontrib>Eimer, Stefan</creatorcontrib><creatorcontrib>Wanker, Erich E</creatorcontrib><creatorcontrib>Klopfenstein, Dieter Robert</creatorcontrib><creatorcontrib>Jahn, Reinhard</creatorcontrib><title>Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Axonal Transport</subject><subject>Axons</subject><subject>Axons - metabolism</subject><subject>Binding sites</subject><subject>Biological Sciences</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Cell membranes</subject><subject>cytoplasmic streaming</subject><subject>exocytosis</subject><subject>Freight</subject><subject>genetics</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>kinesin</subject><subject>Kinesin - metabolism</subject><subject>Kinesins</subject><subject>metabolism</subject><subject>molecular motor proteins</subject><subject>Munc18 Proteins</subject><subject>Munc18 Proteins - metabolism</subject><subject>Mutant Proteins</subject><subject>Mutant Proteins - metabolism</subject><subject>Mutation</subject><subject>Mutation - genetics</subject><subject>Nematodes</subject><subject>nerve tissue</subject><subject>Nerve Tissue Proteins</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons</subject><subject>Neuropeptides</subject><subject>Neuropeptides - metabolism</subject><subject>Neurosecretory cells</subject><subject>PC12 cells</subject><subject>Phosphorylation</subject><subject>plasma membrane</subject><subject>Protein Binding</subject><subject>protein kinases</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>serine</subject><subject>synapse</subject><subject>Syntaxin 1</subject><subject>Syntaxin 1 - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks1vEzEQxVcIREPhzAmwOHHZdsb2eu1LJVTxJSqBBD1bjtebONrYi71BzX-PQ0ICXHqxR_Jvnmb8XlU9R7hAaNnlGEy-QEQmUSGoB9WsnFgLruBhNQOgbS055WfVk5xXAKAaCY-rM0p5gwraWeW-LmMelzFtBzP5GOrkFptSuo6YuxjMQDo3utC5MJEpmZDHmCYSe5K3YTJ3PhAkPpO16_zvpvmWGPLZB5d9qJGYzoyTS0-rR70Zsnt2uM-r2_fvvl9_rG--fPh0_famtoLSqZ6znjNmEO2cS0YBLbTWlbKjTlAw1nDDgQFDaRrbg-osY6oxgnPbIDh2Xl3tdcfNvIxky9TJDHpMfm3SVkfj9b8vwS_1Iv7UjFHBBRaBNweBFH9sXJ702mfrhsEEFzdZoxCs4S0ouB-lxRRoQcr70eIMB4FSFfT1f-gqblLxIWuliqusgAW63EM2xZyT648bIuhdLvQuF_qUi9Lx8u-POfJ_glCAVwdg13mSUxob3UhBC_FiT6zyFNMR4dhISRtxUuhN1GaRfNa334qHHABbIZVivwAq0tB2</recordid><startdate>20120410</startdate><enddate>20120410</enddate><creator>Chua, John Jia En</creator><creator>Butkevich, Eugenia</creator><creator>Worseck, Josephine M</creator><creator>Kittelmann, Maike</creator><creator>Grønborg, Mads</creator><creator>Behrmann, Elmar</creator><creator>Stelzl, Ulrich</creator><creator>Pavlos, Nathan J</creator><creator>Lalowski, Maciej M</creator><creator>Eimer, Stefan</creator><creator>Wanker, Erich E</creator><creator>Klopfenstein, Dieter Robert</creator><creator>Jahn, Reinhard</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20120410</creationdate><title>Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter</title><author>Chua, John Jia En ; Butkevich, Eugenia ; Worseck, Josephine M ; Kittelmann, Maike ; Grønborg, Mads ; Behrmann, Elmar ; Stelzl, Ulrich ; Pavlos, Nathan J ; Lalowski, Maciej M ; Eimer, Stefan ; Wanker, Erich E ; Klopfenstein, Dieter Robert ; Jahn, Reinhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c622t-b3f433a11cb483201c07ce483d2e620aca4a4030318a5cf09dc3395a644c510e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Adaptor Proteins, Signal Transducing - 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Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chua, John Jia En</au><au>Butkevich, Eugenia</au><au>Worseck, Josephine M</au><au>Kittelmann, Maike</au><au>Grønborg, Mads</au><au>Behrmann, Elmar</au><au>Stelzl, Ulrich</au><au>Pavlos, Nathan J</au><au>Lalowski, Maciej M</au><au>Eimer, Stefan</au><au>Wanker, Erich E</au><au>Klopfenstein, Dieter Robert</au><au>Jahn, Reinhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2012-04-10</date><risdate>2012</risdate><volume>109</volume><issue>15</issue><spage>5862</spage><epage>5867</epage><pages>5862-5867</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Presynaptic nerve terminals are formed from preassembled vesicles that are delivered to the prospective synapse by kinesin-mediated axonal transport. However, precisely how the various cargoes are linked to the motor proteins remains unclear. Here, we report a transport complex linking syntaxin 1a (Stx) and Munc18, two proteins functioning in synaptic vesicle exocytosis at the presynaptic plasma membrane, to the motor protein Kinesin-1 via the kinesin adaptor FEZ1. Mutation of the FEZ1 ortholog UNC-76 in Caenorhabditis elegans causes defects in the axonal transport of Stx. We also show that binding of FEZ1 to Kinesin-1 and Munc18 is regulated by phosphorylation, with a conserved site (serine 58) being essential for binding. When expressed in C. elegans, wild-type but not phosphorylation-deficient FEZ1 (S58A) restored axonal transport of Stx. We conclude that FEZ1 operates as a kinesin adaptor for the transport of Stx, with cargo loading and unloading being regulated by protein kinases.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22451907</pmid><doi>10.1073/pnas.1113819109</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Adaptor Proteins, Signal Transducing - metabolism Amino acids Animals Antibodies Axonal Transport Axons Axons - metabolism Binding sites Biological Sciences Caenorhabditis elegans Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins Caenorhabditis elegans Proteins - metabolism Cell membranes cytoplasmic streaming exocytosis Freight genetics HEK293 Cells Humans kinesin Kinesin - metabolism Kinesins metabolism molecular motor proteins Munc18 Proteins Munc18 Proteins - metabolism Mutant Proteins Mutant Proteins - metabolism Mutation Mutation - genetics Nematodes nerve tissue Nerve Tissue Proteins Nerve Tissue Proteins - metabolism Neurons Neuropeptides Neuropeptides - metabolism Neurosecretory cells PC12 cells Phosphorylation plasma membrane Protein Binding protein kinases Protein Transport Proteins serine synapse Syntaxin 1 Syntaxin 1 - metabolism |
| title | Phosphorylation-regulated axonal dependent transport of syntaxin 1 is mediated by a Kinesin-1 adapter |
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