{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T08:01:50Z","timestamp":1791273710580,"version":"4.1.0"},"reference-count":87,"publisher":"Rockefeller University Press","issue":"6","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1998,12,14]]},"abstract":"<jats:p>Neural cell adhesion molecules composed of immunoglobulin and fibronectin type III-like domains have been implicated in cell adhesion, neurite outgrowth, and fasciculation. Axonin-1 and Ng cell adhesion molecule (NgCAM), two molecules with predominantly axonal expression exhibit homophilic interactions across the extracellular space (axonin- 1\/axonin-1 and NgCAM\/NgCAM) and a heterophilic interaction (axonin-1\u2013NgCAM) that occurs exclusively in the plane of the same membrane (cis-interaction). Using domain deletion mutants we localized the NgCAM homophilic binding in the Ig domains 1-4 whereas heterophilic binding to axonin-1 was localized in the Ig domains 2-4 and the third FnIII domain. The NgCAM\u2013NgCAM interaction could be established simultaneously with the axonin-1\u2013NgCAM interaction. In contrast, the axonin-1\u2013NgCAM interaction excluded axonin-1\/axonin-1 binding. These results and the examination of the coclustering of axonin-1 and NgCAM at cell contacts, suggest that intercellular contact is mediated by a symmetric axonin-12\/NgCAM2 tetramer, in which homophilic NgCAM binding across the extracellular space occurs simultaneously with a cis-heterophilic interaction of axonin-1 and NgCAM. The enhanced neurite fasciculation after overexpression of NgCAM by adenoviral vectors indicates that NgCAM is the limiting component for the formation of the axonin-12\/NgCAM2 complexes and, thus, neurite fasciculation in DRG neurons.<\/jats:p>","DOI":"10.1083\/jcb.143.6.1673","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"1673-1690","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":92,"title":["Neurite Fasciculation Mediated by Complexes of Axonin-1 and Ng Cell Adhesion Molecule"],"prefix":"10.1083","volume":"143","author":[{"given":"Stefan","family":"Kunz","sequence":"first","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marianne","family":"Spirig","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia","family":"Ginsburg","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Buchstaller","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philipp","family":"Berger","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rainer","family":"Lanz","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, University of Zurich, CH-8057 Zurich, 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