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First published online 29 May 2007
doi: 10.1242/jcs.006247

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Non-classical export of epimorphin and its adhesion to v-integrin in regulation of epithelial morphogenesis

¹ Department of Morphoregulation, Institute for Frontier Medical Sciences, Kyoto University, 53 Kawahara-cho, Shogoin, Sakyo-ku, Kyoto 606-8507, Japan
² Life Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, MS 977, Berkeley, CA 94720, USA
³ Mayo Clinic Cancer Center, 4500 San Pablo Road, Jacksonville, FL 32224, USA
⁴ Mayo Clinic Proteomics Research Center, 200 First St. SW, Rochester, MN 55905, USA

^* Author for correspondence (e-mail: hirai-yohei{at}frontier.kyoto-u.ac.jp)

Accepted 17 April 2007

Epimorphin (also known as syntaxin 2) acts as an epithelial morphogen when secreted by stromal cells of the mammary gland, lung, liver, colon, pancreas and other tissues, but the same molecule functions within the cell to mediate membrane fusion. How this molecule, which lacks a signal sequence and contains a transmembrane domain at the C-terminus, translocates across the plasma membrane and is secreted to become a morphogen, and how it initiates morphogenic events is not clear. Here, we show that epimorphin is secreted through a non-classical mechanism, similar to that previously described for secretion of the leaderless protein FGF1, and we identify the key molecular elements responsible for translocation and secretion from the cell. We also show that secreted epimorphin binds to v-integrin-containing receptors on target epithelial cells, leading to activation of specific downstream signaling pathways and induction of epithelial morphogenesis. These findings provide key insight into how epimorphin functions as an epithelial morphogen.

Key words: Epimorphin, Integrin, Morphogenesis, Membrane translocation, t-SNARE

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