{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,7]],"date-time":"2025-07-07T06:03:37Z","timestamp":1751868217515},"reference-count":24,"publisher":"The Company of Biologists","issue":"3","license":[{"start":{"date-parts":[[1996,3,1]],"date-time":"1996-03-01T00:00:00Z","timestamp":825638400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1996,3,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>The glycosyl-phosphatidylinositol (GPI)-anchored F3 molecule, a member of the Ig superfamily made up of Ig and FNIII-like domains, is involved in cell-cell adhesion, neuronal pathfinding and fasciculation. Little is known about the mechanism(s) that governs the F3-mediated cellcell recognition. In particular, it is not known whether F3 transduces signals across the membrane.<\/jats:p>\n               <jats:p>Here we show that in F3-transfected CHO cells (1A cells) an increase in tyrosine phosphorylation occurs during F3-mediated aggregation. Moreover, under aggregation conditions F3 immunoprecipitated from 32P-metabolically labeled 1A cells associated with three major phosphorylated proteins. Interestingly, genistein inhibited the F3-mediated aggregation. Increased tyrosine phosphorylation was also observed using antibody-mediated F3-crosslinking. Furtheremore, F3 expressed both in 1A cells and in post-natal mouse cerebellum forms non-covalent soluble complexes with protein tyrosine kinase(s). In cerebellum the F3-associated kinase was identified as fyn. By contrast, a truncated F3 protein, expressed in CHO cells, from which all the FN type III repeats have been deleted, does not associate with a kinase. Cross-linking of the F3-truncated form does not induce modulation of tyrosine phosphorylation. Taken together these data demonstrate that F3 is a molecule that transduces signals through both association with protein tyrosine kinase and modulation of protein tyrosine phosphorylation. The presence of FN type III domains is essential for the activation of the intracellular signaling pathway.<\/jats:p>","DOI":"10.1242\/jcs.109.3.699","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T12:34:29Z","timestamp":1619354069000},"page":"699-704","source":"Crossref","is-referenced-by-count":19,"title":["The GPI-anchored adhesion molecule F3 induces tyrosine phosphorylation: involvement of the FNIII repeats"],"prefix":"10.1242","volume":"109","author":[{"given":"Melchiorre","family":"Cervello","sequence":"first","affiliation":[{"name":"2 Istituto di Biologia dello Sviluppo del Consiglio Nazionale delle Ricerche, Via Archirafi, 20, 90123 Palermo, Italia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Valeria","family":"Matranga","sequence":"additional","affiliation":[{"name":"2 Istituto di Biologia dello Sviluppo del Consiglio Nazionale delle Ricerche, Via Archirafi, 20, 90123 Palermo, Italia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pascal","family":"Durbec","sequence":"additional","affiliation":[{"name":"1 Laboratoire de G\u00e9n\u00e9tique et de Physiologie du D\u00e9veloppement, UMR C 9943, Facult\u00e9 des sciences de Luminy, Case 907, 13288 Marseille Cedex 9, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Genevi\u00e8ve","family":"Rougon","sequence":"additional","affiliation":[{"name":"1 Laboratoire de G\u00e9n\u00e9tique et de Physiologie du D\u00e9veloppement, UMR C 9943, Facult\u00e9 des sciences de Luminy, Case 907, 13288 Marseille Cedex 9, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sophie","family":"Gomez","sequence":"additional","affiliation":[{"name":"1 Laboratoire de G\u00e9n\u00e9tique et de Physiologie du D\u00e9veloppement, UMR C 9943, Facult\u00e9 des sciences de Luminy, Case 907, 13288 Marseille Cedex 9, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1996,3,1]]},"reference":[{"key":"2023122623543359800_JOCES_109_3_699C1","doi-asserted-by":"publisher","first-page":"825","DOI":"10.1083\/jcb.127.3.825","article-title":"NCAM-dependent neurite outgrowth is inhibited in neurons from fyn-minus mice","volume":"127","author":"Beggs","year":"1994","journal-title":"J. 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Homology with fibronectin type III and immunoglobulin type C domains","volume":"2","author":"Brummendorf","year":"1989","journal-title":"Neuron"},{"key":"2023122623543359800_JOCES_109_3_699C4","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1016\/0896-6273(93)90172-N","article-title":"The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin","volume":"10","author":"Brummendorf","year":"1993","journal-title":"Neuron"},{"key":"2023122623543359800_JOCES_109_3_699C5","first-page":"49","article-title":"Signal transduction events underlying neurite outgrowth stimulated by cell adhesion molecules","volume":"4","author":"Doherty","year":"1994","journal-title":"Curr. 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