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- Title
Phosphorylation of Cytohesin-1 by Fyn Is Required for Initiation of Myelination and the Extent of Myelination During Development.
- Authors
Junji Yamauchi; Yuki Miyamoto; Tomohiro Torii; Shou Takashima; Kazumi Kondo; Katsumasa Kawahara; Noriko Nemoto; Chan, Jonah R.; Gozoh Tsujimoto; Akito Tanoue
- Abstract
Schwann cells respond to cues from axons by transforming their cellularmorphology and forming myelin. We demonstrated that the guanine nucleotide exchange factor (GEF) cytohesin-1 promoted myelination by activating the small guanosine triphosphatase (GTPase) Arf6. In mice, ablating cytohesin-1 delayed myelination and diminished the amount of myelin produced. We determined that the Src-family kinase Fyn phosphorylated tyrosine 382 (Y382) of cytohesin-1, and we generated transgenic mice that expressed a Schwann cell-specific phosphorylationmutant of cytohesin-1 (Y382F) that could not be targeted by Fyn. During development, these transgenic mice displayed delayedmyelination compared to that of wild-typemice, aswell as a decrease in the amount of myelin produced, similar to that observed in cytohesin-1-/- mice. These findings demonstrate that phosphorylation of cytohesin-1 by Fyn is required for full myelination and suggest that tyrosine phosphorylation of GEFs may be a mechanism to activate small GTPases engaged in cell morphogenesis.
- Publication
Science Signaling, 2012, Vol 5, Issue 243, p1
- ISSN
1945-0877
- Publication type
Article
- DOI
10.1126/scisignal.2002802