Truncation of the Projection Domain of MAP4 (Microtubule-Associated Protein 4) Leads to Attenuation of Microtubule Dynamic Instability
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- Permana Sofy
- Division of Biological Sciences, Graduate School of Science, Nagoya University Department of Biology, Faculty of Mathematics and Natural Sciences, Brawijaya University
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- Hisanaga Shin-ichi
- Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University
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- Nagatomo Yoko
- Division of Biological Sciences, Graduate School of Science, Nagoya University
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- Iida Junko
- Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University
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- Hotani Hirokazu
- Division of Biological Sciences, Graduate School of Science, Nagoya University
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- Itoh Tomohiko J.
- Division of Biological Sciences, Graduate School of Science, Nagoya University
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抄録
MAP4, a ubiquitous heat-stable MAP, is composed of an asymmetric structure common to the heat-stable MAPs, consisting of an N-terminal projection (PJ) domain and a C-terminal microtubule (MT)-binding (MTB) domain. Although the MTB domain has been intensively studied, the role of the PJ domain, which protrudes from MT-wall and does not bind to MTs, remains unclear. We investigated the roles of the PJ domain on the dynamic instability of MTs by dark-field microscopy using various PJ domain deletion constructs of human MAP4 (PJ1, PJ2, Na-MTB and KDM-MTB). There was no obvious difference in the dynamic instability between the wtMAP4 and any fragments at 0.1 μM, the minimum concentration required to stabilize MTs. The individual MTs stochastically altered between polymerization and depolymerization phases with similar profiles of length change as had been observed in the presence of MAP2 or tau. We also examined the effects at the increased concentrations of 0.7 μM, and found that in some cases the dynamic instability was almost entirely attenuated. The length of both the polymerization and depolymerization phases decreased and “pause-phases” were occasionally observed, especially in the case of PJ1, PJ2 or Na-MTB. No obvious change was observed in the increased concentration of wtMAP4 and KDM-MTB. Additionally, the profiles of MT length change were quite different in 0.7 μM PJ2. Relatively rapid and long depolymerization phases were sometimes observed among quite slow length changes. Perhaps, this unusual profile could be due to the uneven distribution of PJ2 along the MT lattice. These results indicate that the PJ domain of MAP4 participates in the regulation of the dynamic instability.<br>
収録刊行物
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- Cell Structure and Function
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Cell Structure and Function 29 (5/6), 147-157, 2005
日本細胞生物学会
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詳細情報 詳細情報について
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- CRID
- 1390001204696336768
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- NII論文ID
- 130004137489
- 30023110284
- 10015462493
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- NII書誌ID
- AA0060007X
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- ISSN
- 13473700
- 03867196
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- NDL書誌ID
- 7298233
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- PubMed
- 15840946
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 使用不可