Microtubule Association of the Neuronal p35 Activator of Cdk5
Cdk5 and its neuronal activator p35 play an important role in neuronal migration and proper development of the brain cortex. We show that p35 binds directly to α/β-tubulin and microtubules. Microtubule polymers but not the α/β-tubulin heterodimer block p35 interaction with Cdk5 and therefore inhibit...
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| Veröffentlicht in: | The Journal of biological chemistry 2007-06, Vol.282 (26), p.18666-18670 |
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| container_issue | 26 |
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| container_title | The Journal of biological chemistry |
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| creator | Hou, Zhibo Li, Qing He, Lisheng Lim, Hui-Ying Fu, Xinrong Cheung, Nam Sang Qi, Donna X. Qi, Robert Z. |
| description | Cdk5 and its neuronal activator p35 play an important role in neuronal migration and proper development of the brain cortex. We show that p35 binds directly to α/β-tubulin and microtubules. Microtubule polymers but not the α/β-tubulin heterodimer block p35 interaction with Cdk5 and therefore inhibit Cdk5-p35 activity. p25, a neurotoxin-induced and truncated form of p35, does not have tubulin and microtubule binding activities, and Cdk5-p25 is inert to the inhibitory effect of microtubules. p35 displays strong activity in promoting microtubule assembly and inducing formation of microtubule bundles. Furthermore, microtubules stabilized by p35 are resistant to cold-induced disassembly. In cultured cortical neurons, a significant proportion of p35 localizes to microtubules. When microtubules were isolated from rat brain extracts, p35 co-assembled with microtubules, including cold-stable microtubules. Together, these findings suggest that p35 is a microtubule-associated protein that modulates microtubule dynamics. Also, microtubules play an important role in the control of Cdk5 activation. |
| doi_str_mv | 10.1074/jbc.C700052200 |
| format | Article |
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We show that p35 binds directly to α/β-tubulin and microtubules. Microtubule polymers but not the α/β-tubulin heterodimer block p35 interaction with Cdk5 and therefore inhibit Cdk5-p35 activity. p25, a neurotoxin-induced and truncated form of p35, does not have tubulin and microtubule binding activities, and Cdk5-p25 is inert to the inhibitory effect of microtubules. p35 displays strong activity in promoting microtubule assembly and inducing formation of microtubule bundles. Furthermore, microtubules stabilized by p35 are resistant to cold-induced disassembly. In cultured cortical neurons, a significant proportion of p35 localizes to microtubules. When microtubules were isolated from rat brain extracts, p35 co-assembled with microtubules, including cold-stable microtubules. Together, these findings suggest that p35 is a microtubule-associated protein that modulates microtubule dynamics. Also, microtubules play an important role in the control of Cdk5 activation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.C700052200</identifier><identifier>PMID: 17491008</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Brain - cytology ; Cyclin-Dependent Kinase 5 - metabolism ; Humans ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; Microtubules - metabolism ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Neurons - enzymology ; Rats ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Tubulin - metabolism</subject><ispartof>The Journal of biological chemistry, 2007-06, Vol.282 (26), p.18666-18670</ispartof><rights>2007 © 2007 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-40db9f5d36ff3fb5a5d50d7480e972d871ce6189b7d7898fa2cf84191d601c493</citedby><cites>FETCH-LOGICAL-c508t-40db9f5d36ff3fb5a5d50d7480e972d871ce6189b7d7898fa2cf84191d601c493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17491008$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hou, Zhibo</creatorcontrib><creatorcontrib>Li, Qing</creatorcontrib><creatorcontrib>He, Lisheng</creatorcontrib><creatorcontrib>Lim, Hui-Ying</creatorcontrib><creatorcontrib>Fu, Xinrong</creatorcontrib><creatorcontrib>Cheung, Nam Sang</creatorcontrib><creatorcontrib>Qi, Donna X.</creatorcontrib><creatorcontrib>Qi, Robert Z.</creatorcontrib><title>Microtubule Association of the Neuronal p35 Activator of Cdk5</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Cdk5 and its neuronal activator p35 play an important role in neuronal migration and proper development of the brain cortex. 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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Animals Brain - cytology Cyclin-Dependent Kinase 5 - metabolism Humans Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Microtubules - metabolism Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Neurons - enzymology Rats Recombinant Proteins - genetics Recombinant Proteins - metabolism Tubulin - metabolism |
| title | Microtubule Association of the Neuronal p35 Activator of Cdk5 |
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