Functional Analyses of a Neural Cell Specific Variant of Microtubule-Associated Protein 4

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概要

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• The present study was conducted to analyze the functions of a recently reported neural cell specific variant of MAP4 (MAP4-SP) that lacks 72 consecutive amino acid residues in a region that is rich in proline and basic residues (pro-rich region). Although our previous study (Matsushima et al., 2005)^<12)>, using the microtubule-binding domains of the isoform and wild type MAP4 (MAP4-LP), demonstrated a difference in the microtubule bundling activity of the two proteins, here, using the full-length forms of the MAP4 proteins, we show that the proteins do not differ in their microtubule bundling activity both in vitro and in vivo. Expression of the MAP4 proteins, as C-terminal fusions to green fluorescent protein (GFP), in neuroblastoma cells revealed that MAP4-SP decorated microtubules were more remarkable in appearance than MAP4-LP decorated microtubules in the neuronal growth cones. Moreover, a microtubule destabilizing protein, septin2, which interacts with the pro-rich region of MAP4, was more active in destabilizing MAP4-SP-microtubules than MAP4-LP-microtubules in vitro. The susceptibility of MAP4-SP microtubules to destabilization by septin could be attributed to the weaker binding affinity of MAP4-SP for microtubules, as was reported earlier. Taken together, the current findings suggest the possibility that the neural MAP4, with its short pro-rich region, could be important in maintaining more dynamic microtubules in neural cells, and thus allowing more plasticity in and rapid morphological changes of these cells.

• 神奈川大学の論文
• 2006-05-25

著者

• NAKAGAWA Hiroyuki

  Department of Pathology, Kansai Medical University

• KOTANI Susumu

  Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineeri

• Yue Jin

  Department Of Bioscience And Bioinformatics Kyushu Institute Of Technology

• Hasan Mohammad

  Department of Bioscience and Bioinformatics, Kyushu Institute of Technology

• Matsushima Kazuyuki

  Department of Biological Sciences, Faculty of Science, Kanagawa University

• Miyamoto Shigeaki

  Department of Bioscience and Bioinformatics, Kyushu Institute of Technology

• Hasan Mohammad

  Univ. British Columbia British Columbia Can

• Nakagawa Hiroyuki

  Department Of Applied Chemistry School Of Science And Engineering Waseda University

• Matsushima Kazuyuki

  Department Of Biological Sciences Faculty Of Science-city Kanagawa University

• Kotani Susumu

  Kanagawa Univ. Kanagawa Jpn

• Kotani Susumu

  Department Of Biochemical Engineering And Science Faculty Of Computer Science And Systems Engineerin

• Matsushima K

  Department Of Biological Sciences Faculty Of Science-city Kanagawa University

• Miyamoto Shigeaki

  Kyushu Inst. Technol. Fukuoka Jpn

• Miyamoto Shigeaki

  Department Of Biochemical Science Faculty Of Computer And Systems Engineering Kyushu Institute Of Te

• Kotani S

  Kanagawa Univ. Kanagawa

• Kotani Susumu

  Department Of Biological Sciences Faculty Of Science Kanagawa University

• Matsushima Kazuyuki

  Department Of Biological Sciences Faculty Of Science Kanagawa University

• Nakagawa Hiroyuki

  Dept. of Biology, Fac. of Science, Univ of Fukuoka

• 中川 裕之

  Department of Bioscience and Bioinformatics, Kyushu Institute of Technology

• Miyamoto Shigeaki

  Department of Biochemical Engineering and Science, Faculty of Computer Science and System Engineering, Kyushu Institute of Technology

• HASAN Mohammad

  Department of Bioscience and Bioinformatics, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology

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