Tumor Necrosis Factor Induces Hyperphosphorylation of Kinesin Light Chain and Inhibits Kinesin-Mediated Transport of Mitochondria
The molecular motor kinesin is an ATPase that mediates plus end-directed transport of organelles along microtubules. Although the biochemical properties of kinesin are extensively studied, conclusive data on regulation of kinesin-mediated transport are largely lacking. Previously, we showed that the...
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| Veröffentlicht in: | The Journal of cell biology 2000-06, Vol.149 (6), p.1207-1214 |
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| container_title | The Journal of cell biology |
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| creator | de Vos, Kurt Severin, Fedor van Herreweghe, Franky Vancompernolle, Katia Goossens, Vera Hyman, Anthony Grooten, Johan |
| description | The molecular motor kinesin is an ATPase that mediates plus end-directed transport of organelles along microtubules. Although the biochemical properties of kinesin are extensively studied, conclusive data on regulation of kinesin-mediated transport are largely lacking. Previously, we showed that the proinflammatory cytokine tumor necrosis factor induces perinuclear clustering of mitochondria. Here, we show that tumor necrosis factor impairs kinesin motor activity and hyperphosphorylates kinesin light chain through activation of two putative kinesin light chain kinases. Inactivation of kinesin, hyperphosphorylation of kinesin light chain, and perinuclear clustering of mitochondria exhibit the same p38 mitogen-activated kinase dependence, indicating their functional relationship. These data provide evidence for direct regulation of kinesin-mediated organelle transport by extracellular stimuli via cytokine receptor signaling pathways. |
| doi_str_mv | 10.1083/jcb.149.6.1207 |
| format | Article |
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Although the biochemical properties of kinesin are extensively studied, conclusive data on regulation of kinesin-mediated transport are largely lacking. Previously, we showed that the proinflammatory cytokine tumor necrosis factor induces perinuclear clustering of mitochondria. Here, we show that tumor necrosis factor impairs kinesin motor activity and hyperphosphorylates kinesin light chain through activation of two putative kinesin light chain kinases. Inactivation of kinesin, hyperphosphorylation of kinesin light chain, and perinuclear clustering of mitochondria exhibit the same p38 mitogen-activated kinase dependence, indicating their functional relationship. These data provide evidence for direct regulation of kinesin-mediated organelle transport by extracellular stimuli via cytokine receptor signaling pathways.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.149.6.1207</identifier><identifier>PMID: 10851018</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Animals ; Cell culture techniques ; Cell Line ; Cells ; Cellular biology ; Cytosol ; Enzyme Activation ; Enzyme Inhibitors - pharmacology ; Gliding ; Imidazoles - pharmacology ; Kinesin - metabolism ; Light ; Microtubule-Associated Proteins - metabolism ; Microtubules ; Microtubules - metabolism ; Mitochondria ; Mitochondria - metabolism ; Mitogen-Activated Protein Kinases - metabolism ; Molecular Motor Proteins - metabolism ; Organelles ; Original ; p38 Mitogen-Activated Protein Kinases ; Phosphorylation ; Protein isoforms ; Proteins ; Pyridines - pharmacology ; Receptors, Tumor Necrosis Factor - metabolism ; Signal Transduction ; Tumor Necrosis Factor-alpha - pharmacology ; Tumor necrosis factors ; Tumors</subject><ispartof>The Journal of cell biology, 2000-06, Vol.149 (6), p.1207-1214</ispartof><rights>Copyright 2000 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Jun 12, 2000</rights><rights>2000 The Rockefeller University Press 2000 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-e36188a1f907888ad462f93f18957569a84d8c29597a8574be4d264fa745a36a3</citedby><cites>FETCH-LOGICAL-c434t-e36188a1f907888ad462f93f18957569a84d8c29597a8574be4d264fa745a36a3</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/PMC2175118/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175118/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10851018$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Vos, Kurt</creatorcontrib><creatorcontrib>Severin, Fedor</creatorcontrib><creatorcontrib>van Herreweghe, Franky</creatorcontrib><creatorcontrib>Vancompernolle, Katia</creatorcontrib><creatorcontrib>Goossens, Vera</creatorcontrib><creatorcontrib>Hyman, Anthony</creatorcontrib><creatorcontrib>Grooten, Johan</creatorcontrib><title>Tumor Necrosis Factor Induces Hyperphosphorylation of Kinesin Light Chain and Inhibits Kinesin-Mediated Transport of Mitochondria</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The molecular motor kinesin is an ATPase that mediates plus end-directed transport of organelles along microtubules. Although the biochemical properties of kinesin are extensively studied, conclusive data on regulation of kinesin-mediated transport are largely lacking. Previously, we showed that the proinflammatory cytokine tumor necrosis factor induces perinuclear clustering of mitochondria. Here, we show that tumor necrosis factor impairs kinesin motor activity and hyperphosphorylates kinesin light chain through activation of two putative kinesin light chain kinases. Inactivation of kinesin, hyperphosphorylation of kinesin light chain, and perinuclear clustering of mitochondria exhibit the same p38 mitogen-activated kinase dependence, indicating their functional relationship. These data provide evidence for direct regulation of kinesin-mediated organelle transport by extracellular stimuli via cytokine receptor signaling pathways.</description><subject>Animals</subject><subject>Cell culture techniques</subject><subject>Cell Line</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Cytosol</subject><subject>Enzyme Activation</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Gliding</subject><subject>Imidazoles - pharmacology</subject><subject>Kinesin - metabolism</subject><subject>Light</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Mitochondria</subject><subject>Mitochondria - metabolism</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Organelles</subject><subject>Original</subject><subject>p38 Mitogen-Activated Protein Kinases</subject><subject>Phosphorylation</subject><subject>Protein isoforms</subject><subject>Proteins</subject><subject>Pyridines - pharmacology</subject><subject>Receptors, Tumor Necrosis Factor - metabolism</subject><subject>Signal Transduction</subject><subject>Tumor Necrosis Factor-alpha - pharmacology</subject><subject>Tumor necrosis factors</subject><subject>Tumors</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1v1DAQxS1ERZfClRNCUQ_cEmzHnxcktKK06hYuy9nyxk7jVdYOtoO0x_7nONoChYPlGc3vPY39AHiDYIOgaD_su12DiGxYgzDkz8AKUQJrgQh8DlYQYlRLiuk5eJnSHkJIOGlfgPMipQgisQIP2_kQYvXVdjEkl6or3eXS33gzdzZV18fJxmkIqZx4HHV2wVehr26dt8n5auPuh1ytB11q7U3RDW7ncvoN1HfWOJ2tqbZR-zSFmBf5ncuhG4I30elX4KzXY7KvH-8L8P3q83Z9XW--fblZf9rUHWlJrm3LkBAa9RJyUQpDGO5l2yMhKadMakGM6LCkkmtBOdlZYjAjveaE6pbp9gJ8PPlO8-5gTWd9jnpUU3QHHY8qaKf-nXg3qPvwU2HEKUKiGLx_NIjhx2xTVgeXOjuO2tswJ8ULhLHEBbz8D9yHOfryuMULCogkL1BzgpaPT9H2fzZBUC3RqhKtKtEqppZoi-Dd0_2f4KcsC_D2BOxTifDvnCEpGGl_ASw2qtg</recordid><startdate>20000612</startdate><enddate>20000612</enddate><creator>de Vos, Kurt</creator><creator>Severin, Fedor</creator><creator>van Herreweghe, Franky</creator><creator>Vancompernolle, Katia</creator><creator>Goossens, Vera</creator><creator>Hyman, Anthony</creator><creator>Grooten, Johan</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>5PM</scope></search><sort><creationdate>20000612</creationdate><title>Tumor Necrosis Factor Induces Hyperphosphorylation of Kinesin Light Chain and Inhibits Kinesin-Mediated Transport of Mitochondria</title><author>de Vos, Kurt ; 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Cell culture techniques Cell Line Cells Cellular biology Cytosol Enzyme Activation Enzyme Inhibitors - pharmacology Gliding Imidazoles - pharmacology Kinesin - metabolism Light Microtubule-Associated Proteins - metabolism Microtubules Microtubules - metabolism Mitochondria Mitochondria - metabolism Mitogen-Activated Protein Kinases - metabolism Molecular Motor Proteins - metabolism Organelles Original p38 Mitogen-Activated Protein Kinases Phosphorylation Protein isoforms Proteins Pyridines - pharmacology Receptors, Tumor Necrosis Factor - metabolism Signal Transduction Tumor Necrosis Factor-alpha - pharmacology Tumor necrosis factors Tumors |
| title | Tumor Necrosis Factor Induces Hyperphosphorylation of Kinesin Light Chain and Inhibits Kinesin-Mediated Transport of Mitochondria |
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