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J. Biol. Chem., Vol. 275, Issue 48, 37957-37965, December 1, 2000

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Molecular Characterization of CRMP5, a Novel Member of the Collapsin Response Mediator Protein Family^*

Masahide Fukada^§¶, Ikuko Watakabe^¶, Junichi Yuasa-Kawada^§, Hiroyuki Kawachi, Asato Kuroiwa, Yoichi Matsuda^**, and Masaharu Noda^§

From the  Division of Molecular Neurobiology, National Institute for Basic Biology, and ^§ Department of Molecular Biomechanics, Graduate University for Advanced Studies, Okazaki 444-8585, Japan,  Laboratory of Cytogenetics, Division of Bioscience, Graduate School of Environmental Earth Science, and ^** Chromosome Research Unit, Faculty of Science, Hokkaido University, North 10, West 8, Kita-ku, Sapporo 060-0810, Japan

The CRMP (collapsin response mediator protein) family is thought to play key roles in growth cone guidance during neural development. The four members (CRMP1-4) identified to date have been demonstrated to form hetero-multimeric structures through mutual associations. In this study, we cloned a novel member of this family, which we call CRMP5, by the yeast two-hybrid method. This protein shares relatively low amino acid identity with the other CRMP members (49-50%) and also with dihydropyrimidinase (51%), whereas CRMP1-4 exhibit higher identity with each other (68-75%), suggesting that CRMP5 might be categorized into a third subfamily. The mouse CRMP5 gene was located at chromosome 5 B1. Northern blot and in situ hybridization analyses indicated that CRMP5 is expressed throughout the nervous system similarly to the other members (especially CRMP1 and CRMP4) with the expression peak in the first postnatal week. Association experiments using the yeast two-hybrid method and co-immunoprecipitation showed that CRMP5 interacts with dihydropyrimidinase and all the CRMPs including itself, except for CRMP1, although the expression profile almost overlaps with that of CRMP1 during development. These results suggest that CRMP complexes in the developing nervous system are classifiable into two populations that contain either CRMP1 or CRMP5. This indicates that different complexes may have distinct functions in shaping the neural networks.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF249294, AF249295, and AF249296.

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