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Originally published In Press as doi:10.1074/jbc.M302186200 on May 28, 2003

J. Biol. Chem., Vol. 278, Issue 32, 29609-29618, August 8, 2003
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The Number of Repeat Sequences in Microtubule-associated Protein 4 Affects the Microtubule Surface Properties*

Kiyotaka Tokuraku {ddagger} §, Kazuyuki Matsushima ¶, Takanori Matui ¶, Hiroyuki Nakagawa ¶, Miho Katsuki ||, Rie Majima ¶ and Susumu Kotani ¶

From the {ddagger}Department of Chemical Science and Engineering, Miyakonojo National College of Technology, 473-1 Yoshio-cho, Miyakonojo, Miyazaki 885-8567, the Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Fukuoka 820-8502, and the ||Brain Science Institute, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-0198, Japan

The microtubule-binding domain of MAP4, a ubiquitous microtubule-associated protein, contains a Repeat region with tandemly organized repeat sequences. In this study, we focused on the variations of the Repeat region, and searched for MAP4 isoforms with diverse Repeat region organizations. We successfully isolated four types of MAP4 cDNAs, which differed from each other in both the number and the arrangement of the repeat sequences, from a single source (bovine adrenal gland). To examine the functional differences among the isoforms, we prepared the microtubule-binding domain polypeptides of three of the four isoforms, and examined their activities. The isoform fragments showed similar degrees of microtubule assembly promoting activity and microtubule binding affinity. This result suggested that the Repeat region variation is not important for the control of microtubule dynamics, which is believed to be the main function of MAPs. On the other hand, the microtubule bundle-forming activity differed among the isoform fragments. The bundle formation was augmented by increasing the number of repeat sequences in the fragments. Based on these results, we propose the hypothesis that the role of the MAP4 isoforms is to regulate the surface charge of microtubules.


Received for publication, March 3, 2003 , and in revised form, May 21, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB079579, AB079580, AB079581, and AB079582 for R5/clone1, R3/clone2, R4{alpha}, and R4{beta}, respectively.

* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed. Tel.: 81-986-47-1221; Fax: 81-986-47-1231; E-mail: tokuraku{at}miyakonojo-nct.ac.jp.


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K. Tokuraku, T. Q.P. Noguchi, M. Nishie, K. Matsushima, and S. Kotani
An Isoform of Microtubule-associated Protein 4 Inhibits Kinesin-driven Microtubule Gliding
J. Biochem., April 1, 2007; 141(4): 585 - 591.
[Abstract] [Full Text] [PDF]




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