The role of myosin phosphorylation in anaphase chromosome movement
This work deals with the role of myosin phosphorylation in anaphase chromosome movement. Y27632 and ML7 block two different pathways for phosphorylation of the myosin regulatory light chain (MRLC). Both stopped or slowed chromosome movement when added to anaphase crane-fly spermatocytes. To confirm...
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| Veröffentlicht in: | European journal of cell biology 2013-04, Vol.92 (4-5), p.175-186 |
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| creator | Sheykhani, Rozhan Shirodkar, Purnata V. Forer, Arthur |
| description | This work deals with the role of myosin phosphorylation in anaphase chromosome movement. Y27632 and ML7 block two different pathways for phosphorylation of the myosin regulatory light chain (MRLC). Both stopped or slowed chromosome movement when added to anaphase crane-fly spermatocytes. To confirm that the effects of the pharmacological agents were on the presumed targets, we studied cells stained with antibodies against mono- or bi-phosphorylated myosin. For all chromosomes whose movements were affected by a drug, the corresponding spindle fibres of the affected chromosomes had reduced levels of 1P- and 2P-myosin. Thus the drugs acted on the presumed target and myosin phosphorylation is involved in anaphase force production.
Calyculin A, an inhibitor of MRLC dephosphorylation, reversed and accelerated the altered movements caused by Y27632 and ML-7, suggesting that another phosphorylation pathway is involved in phosphorylation of spindle myosin. Staurosporine, a more general phosphorylation inhibitor, also reduced the levels of MRLC phosphorylation and caused anaphase chromosomes to stop or slow. The effects of staurosporine on chromosome movements were not reversed by Calyculin A, confirming that another phosphorylation pathway is involved in phosphorylation of spindle myosin. |
| doi_str_mv | 10.1016/j.ejcb.2013.02.002 |
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Calyculin A, an inhibitor of MRLC dephosphorylation, reversed and accelerated the altered movements caused by Y27632 and ML-7, suggesting that another phosphorylation pathway is involved in phosphorylation of spindle myosin. Staurosporine, a more general phosphorylation inhibitor, also reduced the levels of MRLC phosphorylation and caused anaphase chromosomes to stop or slow. The effects of staurosporine on chromosome movements were not reversed by Calyculin A, confirming that another phosphorylation pathway is involved in phosphorylation of spindle myosin.</description><identifier>ISSN: 0171-9335</identifier><identifier>EISSN: 1618-1298</identifier><identifier>DOI: 10.1016/j.ejcb.2013.02.002</identifier><identifier>PMID: 23566798</identifier><language>eng</language><publisher>Germany: Elsevier GmbH</publisher><subject>Amides - pharmacology ; Anaphase ; Animals ; Azepines - pharmacology ; Calyculin A ; Cells, Cultured ; Chromosome movement ; Chromosome Segregation - drug effects ; Chromosome Segregation - physiology ; Chromosomes, Insect - metabolism ; Crane-fly spermatocyte ; Diptera ; Indoles - pharmacology ; Insect Proteins - antagonists & inhibitors ; Insect Proteins - metabolism ; Kinase inhibitor ; Male ; Maleimides - pharmacology ; Myosins - metabolism ; Naphthalenes - pharmacology ; Phosphorylated myosin ; Phosphorylation ; Protein Kinase Inhibitors - pharmacology ; Protein Processing, Post-Translational ; Pyridines - pharmacology ; Single-Cell Analysis ; Spermatocytes - drug effects ; Spermatocytes - physiology ; Spindle Apparatus - metabolism ; Spindle fibre ; Staurosporine - pharmacology</subject><ispartof>European journal of cell biology, 2013-04, Vol.92 (4-5), p.175-186</ispartof><rights>2013 Elsevier GmbH</rights><rights>Copyright © 2013 Elsevier GmbH. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-7da2f1e0f61921738d7deb2220aa0b2184312434abf0e1fa12288790effc3f03</citedby><cites>FETCH-LOGICAL-c433t-7da2f1e0f61921738d7deb2220aa0b2184312434abf0e1fa12288790effc3f03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ejcb.2013.02.002$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23566798$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sheykhani, Rozhan</creatorcontrib><creatorcontrib>Shirodkar, Purnata V.</creatorcontrib><creatorcontrib>Forer, Arthur</creatorcontrib><title>The role of myosin phosphorylation in anaphase chromosome movement</title><title>European journal of cell biology</title><addtitle>Eur J Cell Biol</addtitle><description>This work deals with the role of myosin phosphorylation in anaphase chromosome movement. Y27632 and ML7 block two different pathways for phosphorylation of the myosin regulatory light chain (MRLC). Both stopped or slowed chromosome movement when added to anaphase crane-fly spermatocytes. To confirm that the effects of the pharmacological agents were on the presumed targets, we studied cells stained with antibodies against mono- or bi-phosphorylated myosin. For all chromosomes whose movements were affected by a drug, the corresponding spindle fibres of the affected chromosomes had reduced levels of 1P- and 2P-myosin. Thus the drugs acted on the presumed target and myosin phosphorylation is involved in anaphase force production.
Calyculin A, an inhibitor of MRLC dephosphorylation, reversed and accelerated the altered movements caused by Y27632 and ML-7, suggesting that another phosphorylation pathway is involved in phosphorylation of spindle myosin. Staurosporine, a more general phosphorylation inhibitor, also reduced the levels of MRLC phosphorylation and caused anaphase chromosomes to stop or slow. The effects of staurosporine on chromosome movements were not reversed by Calyculin A, confirming that another phosphorylation pathway is involved in phosphorylation of spindle myosin.</description><subject>Amides - pharmacology</subject><subject>Anaphase</subject><subject>Animals</subject><subject>Azepines - pharmacology</subject><subject>Calyculin A</subject><subject>Cells, Cultured</subject><subject>Chromosome movement</subject><subject>Chromosome Segregation - drug effects</subject><subject>Chromosome Segregation - physiology</subject><subject>Chromosomes, Insect - metabolism</subject><subject>Crane-fly spermatocyte</subject><subject>Diptera</subject><subject>Indoles - pharmacology</subject><subject>Insect Proteins - antagonists & inhibitors</subject><subject>Insect Proteins - metabolism</subject><subject>Kinase inhibitor</subject><subject>Male</subject><subject>Maleimides - pharmacology</subject><subject>Myosins - metabolism</subject><subject>Naphthalenes - pharmacology</subject><subject>Phosphorylated myosin</subject><subject>Phosphorylation</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Protein Processing, Post-Translational</subject><subject>Pyridines - pharmacology</subject><subject>Single-Cell Analysis</subject><subject>Spermatocytes - drug effects</subject><subject>Spermatocytes - physiology</subject><subject>Spindle Apparatus - metabolism</subject><subject>Spindle fibre</subject><subject>Staurosporine - pharmacology</subject><issn>0171-9335</issn><issn>1618-1298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkMFq3DAQQEVoSDZpfyCH4GMvdmdGXluCXtqlTQqBXPYuZHmEvdjWVvIG9u_rZbc9lhyGgeHNOzwhHhAKBKy-7AreuaYgQFkAFQB0JVZYocqRtPogVoA15lrK9a24S2kHgGul9Y24Jbmuqlqrlfi-7TiLYeAs-Gw8htRP2b4LaZl4HOzchylbTnay-84mzlwXwxhSGDkbwxuPPM0fxbW3Q-JPl30vtj9_bDfP-cvr06_Nt5fclVLOed1a8sjgK9SEtVRt3XJDRGAtNISqlEilLG3jgdFbJFKq1sDeO-lB3ovPZ-0-ht8HTrMZ--R4GOzE4ZAMSq01Lm79DnQNShOU5YLSGXUxpBTZm33sRxuPBsGcKpudOVU2p8oGyCyVl6fHi__QjNz-e_mbdQG-ngFeerz1HE1yPU-O2z6ym00b-v_5_wD3HI0d</recordid><startdate>20130401</startdate><enddate>20130401</enddate><creator>Sheykhani, Rozhan</creator><creator>Shirodkar, Purnata V.</creator><creator>Forer, Arthur</creator><general>Elsevier GmbH</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>7X8</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20130401</creationdate><title>The role of myosin phosphorylation in anaphase chromosome movement</title><author>Sheykhani, Rozhan ; Shirodkar, Purnata V. ; Forer, Arthur</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-7da2f1e0f61921738d7deb2220aa0b2184312434abf0e1fa12288790effc3f03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amides - pharmacology</topic><topic>Anaphase</topic><topic>Animals</topic><topic>Azepines - pharmacology</topic><topic>Calyculin A</topic><topic>Cells, Cultured</topic><topic>Chromosome movement</topic><topic>Chromosome Segregation - drug effects</topic><topic>Chromosome Segregation - physiology</topic><topic>Chromosomes, Insect - metabolism</topic><topic>Crane-fly spermatocyte</topic><topic>Diptera</topic><topic>Indoles - pharmacology</topic><topic>Insect Proteins - antagonists & inhibitors</topic><topic>Insect Proteins - metabolism</topic><topic>Kinase inhibitor</topic><topic>Male</topic><topic>Maleimides - pharmacology</topic><topic>Myosins - metabolism</topic><topic>Naphthalenes - pharmacology</topic><topic>Phosphorylated myosin</topic><topic>Phosphorylation</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>Protein Processing, Post-Translational</topic><topic>Pyridines - pharmacology</topic><topic>Single-Cell Analysis</topic><topic>Spermatocytes - drug effects</topic><topic>Spermatocytes - physiology</topic><topic>Spindle Apparatus - metabolism</topic><topic>Spindle fibre</topic><topic>Staurosporine - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sheykhani, Rozhan</creatorcontrib><creatorcontrib>Shirodkar, Purnata V.</creatorcontrib><creatorcontrib>Forer, Arthur</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>European journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sheykhani, Rozhan</au><au>Shirodkar, Purnata V.</au><au>Forer, Arthur</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of myosin phosphorylation in anaphase chromosome movement</atitle><jtitle>European journal of cell biology</jtitle><addtitle>Eur J Cell Biol</addtitle><date>2013-04-01</date><risdate>2013</risdate><volume>92</volume><issue>4-5</issue><spage>175</spage><epage>186</epage><pages>175-186</pages><issn>0171-9335</issn><eissn>1618-1298</eissn><abstract>This work deals with the role of myosin phosphorylation in anaphase chromosome movement. Y27632 and ML7 block two different pathways for phosphorylation of the myosin regulatory light chain (MRLC). Both stopped or slowed chromosome movement when added to anaphase crane-fly spermatocytes. To confirm that the effects of the pharmacological agents were on the presumed targets, we studied cells stained with antibodies against mono- or bi-phosphorylated myosin. For all chromosomes whose movements were affected by a drug, the corresponding spindle fibres of the affected chromosomes had reduced levels of 1P- and 2P-myosin. Thus the drugs acted on the presumed target and myosin phosphorylation is involved in anaphase force production.
Calyculin A, an inhibitor of MRLC dephosphorylation, reversed and accelerated the altered movements caused by Y27632 and ML-7, suggesting that another phosphorylation pathway is involved in phosphorylation of spindle myosin. Staurosporine, a more general phosphorylation inhibitor, also reduced the levels of MRLC phosphorylation and caused anaphase chromosomes to stop or slow. The effects of staurosporine on chromosome movements were not reversed by Calyculin A, confirming that another phosphorylation pathway is involved in phosphorylation of spindle myosin.</abstract><cop>Germany</cop><pub>Elsevier GmbH</pub><pmid>23566798</pmid><doi>10.1016/j.ejcb.2013.02.002</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amides - pharmacology Anaphase Animals Azepines - pharmacology Calyculin A Cells, Cultured Chromosome movement Chromosome Segregation - drug effects Chromosome Segregation - physiology Chromosomes, Insect - metabolism Crane-fly spermatocyte Diptera Indoles - pharmacology Insect Proteins - antagonists & inhibitors Insect Proteins - metabolism Kinase inhibitor Male Maleimides - pharmacology Myosins - metabolism Naphthalenes - pharmacology Phosphorylated myosin Phosphorylation Protein Kinase Inhibitors - pharmacology Protein Processing, Post-Translational Pyridines - pharmacology Single-Cell Analysis Spermatocytes - drug effects Spermatocytes - physiology Spindle Apparatus - metabolism Spindle fibre Staurosporine - pharmacology |
| title | The role of myosin phosphorylation in anaphase chromosome movement |
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