Control of Microtubule Assembly-Disassembly by Calcium-Dependent Regulator Protein
The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1978-08, Vol.75 (8), p.3771-3775 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Marcum, J. Michael Dedman, John R. Brinkley, B. R. Means, Anthony R. |
| description | The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with antitubulin. This characteristic localization in the mitotic half-spindle suggested a role for CDR in the control of microtubule assembly-disassembly during mitosis. Thus, CDR was examined for its effects on microtubule polymerization in vitro. It was determined that stoichiometric concentrations of CDR and a homologous Ca2+-binding protein, skeletal muscle troponin C, both inhibited and reversed microtubule assembly in a Ca2+-dependent manner. CDR-dependent inhibition of in vitro microtubule assembly occurred at physiological Ca2+concentrations (∼ 10 μ M) that, in the absence of CDR, caused only a slight reduction in polymerization. At Ca2+concentrations in the low physiological range ( |
| doi_str_mv | 10.1073/pnas.75.8.3771 |
| format | Article |
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Michael ; Dedman, John R. ; Brinkley, B. R. ; Means, Anthony R.</creator><creatorcontrib>Marcum, J. Michael ; Dedman, John R. ; Brinkley, B. R. ; Means, Anthony R.</creatorcontrib><description>The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with antitubulin. This characteristic localization in the mitotic half-spindle suggested a role for CDR in the control of microtubule assembly-disassembly during mitosis. Thus, CDR was examined for its effects on microtubule polymerization in vitro. It was determined that stoichiometric concentrations of CDR and a homologous Ca2+-binding protein, skeletal muscle troponin C, both inhibited and reversed microtubule assembly in a Ca2+-dependent manner. CDR-dependent inhibition of in vitro microtubule assembly occurred at physiological Ca2+concentrations (∼ 10 μ M) that, in the absence of CDR, caused only a slight reduction in polymerization. At Ca2+concentrations in the low physiological range (<1 μ M), no inhibition was observed. These biochemical results, together with the immunofluorescent localization of CDR in the mitotic half-spindle, provide evidence that Ca2+is an endogenous regulator of microtubule disassembly through the activity of CDR.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.75.8.3771</identifier><identifier>PMID: 211505</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>2',3'-Cyclic-Nucleotide Phosphodiesterases - metabolism ; Anaphase ; Animals ; Calcium - pharmacology ; Calmodulin - pharmacology ; Carrier Proteins - pharmacology ; Gels ; In Vitro Techniques ; Microtubule proteins ; Microtubules ; Microtubules - metabolism ; Mitosis ; Mitotic spindle apparatus ; Muscle spindles ; Parvalbumins - pharmacology ; Phosphoric Diester Hydrolases - metabolism ; Polymerization ; Rats ; Skeletal muscle ; Testes ; Troponin - pharmacology ; Turbidity</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1978-08, Vol.75 (8), p.3771-3775</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c521t-f54e9501acba82e99f8386e6b6969c90dd6fbd88fa806166d7b5c4f226710deb3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/75/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/68764$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/68764$$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/211505$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marcum, J. Michael</creatorcontrib><creatorcontrib>Dedman, John R.</creatorcontrib><creatorcontrib>Brinkley, B. R.</creatorcontrib><creatorcontrib>Means, Anthony R.</creatorcontrib><title>Control of Microtubule Assembly-Disassembly by Calcium-Dependent Regulator Protein</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with antitubulin. This characteristic localization in the mitotic half-spindle suggested a role for CDR in the control of microtubule assembly-disassembly during mitosis. Thus, CDR was examined for its effects on microtubule polymerization in vitro. It was determined that stoichiometric concentrations of CDR and a homologous Ca2+-binding protein, skeletal muscle troponin C, both inhibited and reversed microtubule assembly in a Ca2+-dependent manner. CDR-dependent inhibition of in vitro microtubule assembly occurred at physiological Ca2+concentrations (∼ 10 μ M) that, in the absence of CDR, caused only a slight reduction in polymerization. At Ca2+concentrations in the low physiological range (<1 μ M), no inhibition was observed. These biochemical results, together with the immunofluorescent localization of CDR in the mitotic half-spindle, provide evidence that Ca2+is an endogenous regulator of microtubule disassembly through the activity of CDR.</description><subject>2',3'-Cyclic-Nucleotide Phosphodiesterases - metabolism</subject><subject>Anaphase</subject><subject>Animals</subject><subject>Calcium - pharmacology</subject><subject>Calmodulin - pharmacology</subject><subject>Carrier Proteins - pharmacology</subject><subject>Gels</subject><subject>In Vitro Techniques</subject><subject>Microtubule proteins</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Mitosis</subject><subject>Mitotic spindle apparatus</subject><subject>Muscle spindles</subject><subject>Parvalbumins - pharmacology</subject><subject>Phosphoric Diester Hydrolases - metabolism</subject><subject>Polymerization</subject><subject>Rats</subject><subject>Skeletal muscle</subject><subject>Testes</subject><subject>Troponin - pharmacology</subject><subject>Turbidity</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kTtv2zAUhYkiaeK4XTMUKaApm1SSEl9DhsB5AilaGO1MkNJlqoASHVEq4n9fGnaNZMnEC5zz8V6cg9ApwQXBovy26k0sBCtkUQpBPqAZwYrkvFL4AM0wpiKXFa2O0UmMTxhjxSQ-Qh8pIQyzGVouQj8OwWfBZd_begjjZCcP2WWM0Fm_zq_aaHZzZtfZwvi6nbr8ClbQN9CP2RIeJ2_GMGQ_Ew1t_wkdOuMjfN69c_T75vrX4i5_-HF7v7h8yGtGyZg7VoFimJjaGklBKSdLyYFbrriqFW4a7mwjpTMSc8J5IyyrK0cpFwQ3YMs5utj-u5psB02djhmM16uh7cyw1sG0-q3St3_0Y_irS0Ull4k_3_FDeJ4gjrprYw3emx7CFLWoCKdMlclYbI0pnhgHcPsdBOtNB3rTgRZMS73pIAFnry_b27ehv1q8wf6Le1y7yfsRXsZk_PqeMelftvpTTPnvDVwKXpX_AOx_pZQ</recordid><startdate>19780801</startdate><enddate>19780801</enddate><creator>Marcum, J. Michael</creator><creator>Dedman, John R.</creator><creator>Brinkley, B. R.</creator><creator>Means, Anthony R.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>5PM</scope></search><sort><creationdate>19780801</creationdate><title>Control of Microtubule Assembly-Disassembly by Calcium-Dependent Regulator Protein</title><author>Marcum, J. Michael ; Dedman, John R. ; Brinkley, B. R. ; Means, Anthony R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c521t-f54e9501acba82e99f8386e6b6969c90dd6fbd88fa806166d7b5c4f226710deb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>2',3'-Cyclic-Nucleotide Phosphodiesterases - metabolism</topic><topic>Anaphase</topic><topic>Animals</topic><topic>Calcium - pharmacology</topic><topic>Calmodulin - pharmacology</topic><topic>Carrier Proteins - pharmacology</topic><topic>Gels</topic><topic>In Vitro Techniques</topic><topic>Microtubule proteins</topic><topic>Microtubules</topic><topic>Microtubules - metabolism</topic><topic>Mitosis</topic><topic>Mitotic spindle apparatus</topic><topic>Muscle spindles</topic><topic>Parvalbumins - pharmacology</topic><topic>Phosphoric Diester Hydrolases - metabolism</topic><topic>Polymerization</topic><topic>Rats</topic><topic>Skeletal muscle</topic><topic>Testes</topic><topic>Troponin - pharmacology</topic><topic>Turbidity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marcum, J. Michael</creatorcontrib><creatorcontrib>Dedman, John R.</creatorcontrib><creatorcontrib>Brinkley, B. R.</creatorcontrib><creatorcontrib>Means, Anthony R.</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>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>Marcum, J. Michael</au><au>Dedman, John R.</au><au>Brinkley, B. R.</au><au>Means, Anthony R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Control of Microtubule Assembly-Disassembly by Calcium-Dependent Regulator Protein</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1978-08-01</date><risdate>1978</risdate><volume>75</volume><issue>8</issue><spage>3771</spage><epage>3775</epage><pages>3771-3775</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The Ca2+-dependent regulator (CDR) protein of cyclic nucleotide phosphodiesterase is a low molecular weight, acidic, Ca2+-binding protein which has been implicated in a number of Ca2+-dependent enzymatic functions. Indirect immunofluorescence has revealed that CDR is specifically associated with the chromosome-to-pole region of the mitotic apparatus during metaphase-anaphase in a pattern distinctly different from that of similar cultured cells stained with antitubulin. This characteristic localization in the mitotic half-spindle suggested a role for CDR in the control of microtubule assembly-disassembly during mitosis. Thus, CDR was examined for its effects on microtubule polymerization in vitro. It was determined that stoichiometric concentrations of CDR and a homologous Ca2+-binding protein, skeletal muscle troponin C, both inhibited and reversed microtubule assembly in a Ca2+-dependent manner. CDR-dependent inhibition of in vitro microtubule assembly occurred at physiological Ca2+concentrations (∼ 10 μ M) that, in the absence of CDR, caused only a slight reduction in polymerization. At Ca2+concentrations in the low physiological range (<1 μ M), no inhibition was observed. These biochemical results, together with the immunofluorescent localization of CDR in the mitotic half-spindle, provide evidence that Ca2+is an endogenous regulator of microtubule disassembly through the activity of CDR.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>211505</pmid><doi>10.1073/pnas.75.8.3771</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 2',3'-Cyclic-Nucleotide Phosphodiesterases - metabolism Anaphase Animals Calcium - pharmacology Calmodulin - pharmacology Carrier Proteins - pharmacology Gels In Vitro Techniques Microtubule proteins Microtubules Microtubules - metabolism Mitosis Mitotic spindle apparatus Muscle spindles Parvalbumins - pharmacology Phosphoric Diester Hydrolases - metabolism Polymerization Rats Skeletal muscle Testes Troponin - pharmacology Turbidity |
| title | Control of Microtubule Assembly-Disassembly by Calcium-Dependent Regulator Protein |
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