| First Author | Ikeda W | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 286 |
| Issue | 5 | Pages | 1066-72 |
| PubMed ID | 11527409 | Mgi Jnum | J:76629 |
| Mgi Id | MGI:2179874 | Doi | 10.1006/bbrc.2001.5481 |
| Citation | Ikeda W, et al. (2001) Identification of splicing variants of Frabin with partly different functions and tissue distribution. Biochem Biophys Res Commun 286(5):1066-72 |
| abstractText | Frabin is a GDP/GTP exchange protein for Cdc42 small G protein with actin filament-binding activity. Frabin consists of the actin filament-binding domain, the Dbl homology domain, the first pleckstrin homology domain, the FYVE-finger domain, and the second pleckstrin homology domain in this order from the N-terminus. Frabin forms filopodia through direct activation of Cdc42 and lamellipodia through indirect activation of Rac small G protein. We isolated here two smaller splicing variants of frabin and named the original one, middle-size one, and smallest one frabin-alpha, -beta, and -gamma, respectively. Frabin-beta lacked the second pleckstrin homology domain and frabin-gamma lacked the FYVE-finger domain and the second pleckstrin homology domain. These three variants were expressed in all of the tissues examined but their expression levels are different depending on tissues. In L fibroblasts, all the three variants formed filopodia. As to lamellipodia, frabin-alpha formed them; frabin-beta formed them to a small extent; and frabin-gamma did not. In MDCK epithelial cells, frabin-alpha formed microspikes but frabin-beta or -gamma did not. |
