Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly
Chicken erythrocyte tubulin containing a unique beta tubulin variant polymerizes with greater efficiency (lower critical concentration) but at a slower rate than chicken brain tubulin. In a previous study we demonstrated that the low net rate of assembly is partly due to the presence of large oligom...
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| Veröffentlicht in: | The Journal of biological chemistry 1986-02, Vol.261 (5), p.2319-2324 |
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| container_title | The Journal of biological chemistry |
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| creator | Murphy, D B Wallis, K T |
| description | Chicken erythrocyte tubulin containing a unique beta tubulin variant polymerizes with greater efficiency (lower critical concentration) but at a slower rate than chicken brain tubulin. In a previous study we demonstrated that the low net rate of assembly is partly due to the presence of large oligomers and rings which reduce the initial rate of subunit elongation on microtubule seeds (Murphy, D.B., and Wallis, K.T. (1985) J. Biol. Chem. 260, 12293-12301). In this study we show that erythrocyte tubulin oligomers also retard the rate of microtubule nucleation and the net rate of self-assembly. The inhibitory effect is most likely to be due to the increased stability of erythrocyte tubulin oligomers, including a novel polymer of coiled rings that forms during the rapid phase of microtubule polymerization. The slow rate of dissociation of rings and coils into dimers and small oligomers appears to limit both the nucleation and elongation steps in the self-assembly of erythrocyte microtubules. |
| doi_str_mv | 10.1016/S0021-9258(17)35938-0 |
| format | Article |
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The inhibitory effect is most likely to be due to the increased stability of erythrocyte tubulin oligomers, including a novel polymer of coiled rings that forms during the rapid phase of microtubule polymerization. The slow rate of dissociation of rings and coils into dimers and small oligomers appears to limit both the nucleation and elongation steps in the self-assembly of erythrocyte microtubules.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)35938-0</identifier><identifier>PMID: 3944136</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Cell structures and functions ; Chickens ; Cytoskeleton, cytoplasm. Intracellular movements ; Erythrocytes - metabolism ; Fundamental and applied biological sciences. Psychology ; Guanosine Diphosphate - pharmacology ; Guanosine Triphosphate - pharmacology ; Magnesium - pharmacology ; Microscopy, Electron ; Microtubules - metabolism ; Microtubules - ultrastructure ; Molecular and cellular biology ; Protein Conformation ; Time Factors ; Tubulin - metabolism</subject><ispartof>The Journal of biological chemistry, 1986-02, Vol.261 (5), p.2319-2324</ispartof><rights>1986 © 1986 ASBMB. 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Tubulin oligomers limit the rate of microtubule self-assembly</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Chicken erythrocyte tubulin containing a unique beta tubulin variant polymerizes with greater efficiency (lower critical concentration) but at a slower rate than chicken brain tubulin. In a previous study we demonstrated that the low net rate of assembly is partly due to the presence of large oligomers and rings which reduce the initial rate of subunit elongation on microtubule seeds (Murphy, D.B., and Wallis, K.T. (1985) J. Biol. Chem. 260, 12293-12301). In this study we show that erythrocyte tubulin oligomers also retard the rate of microtubule nucleation and the net rate of self-assembly. The inhibitory effect is most likely to be due to the increased stability of erythrocyte tubulin oligomers, including a novel polymer of coiled rings that forms during the rapid phase of microtubule polymerization. The slow rate of dissociation of rings and coils into dimers and small oligomers appears to limit both the nucleation and elongation steps in the self-assembly of erythrocyte microtubules.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Chickens</subject><subject>Cytoskeleton, cytoplasm. Intracellular movements</subject><subject>Erythrocytes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Guanosine Diphosphate - pharmacology</subject><subject>Guanosine Triphosphate - pharmacology</subject><subject>Magnesium - pharmacology</subject><subject>Microscopy, Electron</subject><subject>Microtubules - metabolism</subject><subject>Microtubules - ultrastructure</subject><subject>Molecular and cellular biology</subject><subject>Protein Conformation</subject><subject>Time Factors</subject><subject>Tubulin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkFFLHDEUhYO02NX2JwiDlKIPY3MnmWTzVIqoLQh9qIW-hUzmxknJbDSZsey_N-uuC31qXi7hfOfewyHkBOgFUBCff1LaQK2adnkG8py1ii1rekAWQJesZi38fkMWe-QdOcr5Dy2PKzgkh0xxDkwsyHCV1tOQol1PWI3epjjN3RywMjnj2IV15VfVk59SvKjuNkr5xuDv44gpV8GPfqqmAatkij-6f1ZkDK5-3fOevHUmZPywm8fk1_XV3eW3-vbHzffLr7e15YzSWvKWYWc49KIxjDHnnHFWQCe54UYywxGAIRgnQMlONYqb4hS9VMpYIdkx-bTd-5Di44x50qPPFkMwK4xz1lKIpeICCthuwRI454ROPyQ_mrTWQPWmYf3SsN7Up0Hql4Y1Lb6T3YG5G7Hfu3aVFv3jTjfZmuCSWVmf95gskYFtzp9uscHfD399Qt35aAccdSNAt7phoAr0ZQthaezJY9LZelxZ7IvBTrqP_j9pnwH2w6TI</recordid><startdate>19860215</startdate><enddate>19860215</enddate><creator>Murphy, D B</creator><creator>Wallis, K T</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>19860215</creationdate><title>Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly</title><author>Murphy, D B ; Wallis, K T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4300-7453eba41d62a333fffafc61b74a4a73a4e113e1af6197b9294ac436d799ac673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Chickens</topic><topic>Cytoskeleton, cytoplasm. Intracellular movements</topic><topic>Erythrocytes - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Guanosine Diphosphate - pharmacology</topic><topic>Guanosine Triphosphate - pharmacology</topic><topic>Magnesium - pharmacology</topic><topic>Microscopy, Electron</topic><topic>Microtubules - metabolism</topic><topic>Microtubules - ultrastructure</topic><topic>Molecular and cellular biology</topic><topic>Protein Conformation</topic><topic>Time Factors</topic><topic>Tubulin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murphy, D B</creatorcontrib><creatorcontrib>Wallis, K T</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murphy, D B</au><au>Wallis, K T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1986-02-15</date><risdate>1986</risdate><volume>261</volume><issue>5</issue><spage>2319</spage><epage>2324</epage><pages>2319-2324</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Chicken erythrocyte tubulin containing a unique beta tubulin variant polymerizes with greater efficiency (lower critical concentration) but at a slower rate than chicken brain tubulin. In a previous study we demonstrated that the low net rate of assembly is partly due to the presence of large oligomers and rings which reduce the initial rate of subunit elongation on microtubule seeds (Murphy, D.B., and Wallis, K.T. (1985) J. Biol. Chem. 260, 12293-12301). In this study we show that erythrocyte tubulin oligomers also retard the rate of microtubule nucleation and the net rate of self-assembly. The inhibitory effect is most likely to be due to the increased stability of erythrocyte tubulin oligomers, including a novel polymer of coiled rings that forms during the rapid phase of microtubule polymerization. The slow rate of dissociation of rings and coils into dimers and small oligomers appears to limit both the nucleation and elongation steps in the self-assembly of erythrocyte microtubules.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3944136</pmid><doi>10.1016/S0021-9258(17)35938-0</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1986-02, Vol.261 (5), p.2319-2324 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Cell structures and functions Chickens Cytoskeleton, cytoplasm. Intracellular movements Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology Guanosine Diphosphate - pharmacology Guanosine Triphosphate - pharmacology Magnesium - pharmacology Microscopy, Electron Microtubules - metabolism Microtubules - ultrastructure Molecular and cellular biology Protein Conformation Time Factors Tubulin - metabolism |
| title | Erythrocyte microtubule assembly in vitro. Tubulin oligomers limit the rate of microtubule self-assembly |
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