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Published online 10 March 2003. doi:10.1083/jcb.200209074
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© The Rockefeller University Press, 0021-9525/2003/3/963 $5.00
The Journal of Cell Biology, Volume 160, Number 6, 963-973

Article

 AMIGO, a transmembrane protein implicated in axon tract development, defines a novel protein family with leucine-rich repeats

Juha Kuja-Panula1, Marjaana Kiiltomäki1, Takashi Yamashiro2, Ari Rouhiainen1,3 and Heikki Rauvala1

1 Department of Biosciences, Institute of Biotechnology, Neuroscience Center
2 Developmental Biology Program, Institute of Biotechnology, University of Helsinki, Helsinki 00014, Finland
3 Finnish Red Cross Blood Transfusion Service, Helsinki 00310, Finland

Address correspondence to Juha Kuja-Panula, Neuroscience Center, Viikinkaari 5, PO Box 56, University of Helsinki, Helsinki 00014, Finland. Tel.: 358-9-19159061. Fax: 358-9-19159068. E-mail: Juha.Kuja-Panula{at}Helsinki.fi; or Heikki Rauvala, Neuroscience Center, Viikinkaari 5, PO Box 56, University of Helsinki, Helsinki 00014, Finland. Tel.: 358-9-19159064. Fax: 358-9-19159068. E-mail: Heikki.Rauvala{at}Helsinki.fi

Ordered differential display identified a novel sequence induced in neurons by the neurite-promoting protein amphoterin. We named this gene amphoterin-induced gene and ORF (AMIGO), and also cloned two other novel genes homologous to AMIGO (AMIGO2 and AMIGO3). Together, these three AMIGOs form a novel family of genes coding for type I transmembrane proteins which contain a signal sequence for secretion and a transmembrane domain. The deduced extracellular parts of the AMIGOs contain six leucine-rich repeats (LRRs) flanked by cysteine-rich LRR NH2- and COOH-terminal domains and by one immunoglobulin domain close to the transmembrane region. A substrate-bound form of the recombinant AMIGO ectodomain promoted prominent neurite extension in hippocampal neurons, and in solution, the same AMIGO ectodomain inhibited fasciculation of neurites. A homophilic and heterophilic binding mechanism is shown between the members of the AMIGO family. Our results suggest that the members of the AMIGO protein family are novel cell adhesion molecules among which AMIGO is specifically expressed on fiber tracts of neuronal tissues and participates in their formation.

Key Words: fasciculation; cell adhesion; neurite outgrowth; Ig superfamily; leucine-rich repeat

* Abbreviations used in this paper: AMIGO, amphoterin-induced gene and ORF; ChrB, chromogranin B; LRR, leucine-rich repeat; ODD, ordered differential display; RAGE, receptor for advanced glycation end products.


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