Fyn-induced phosphorylation of beta-adducin at tyrosine 489 and its role in their subcellular localization.
Fyn is a Src-family tyrosine kinase involved in neuronal development, transmission, and plasticity in mammalian central nervous system. We have previously reported that Fyn binds to a cytoskeletal protein, beta-adducin, in a phosphorylation-dependent manner. In the present report, we show that Fyn phosphorylates beta-adducin at tyrosine 489 located in its C-terminal tail domain. Phosphorylation of beta-adducin at Y489 was required for its association with the Fyn-SH2 domain. An antibody specific to the phosphorylated form of beta-adducin was raised in rabbits and showed that Y489 of beta-adducin was phosphorylated in wild type, but not in Fyn(-/-) mice, suggesting that Y489 of beta-adducin is phosphorylated downstream of Fyn in vivo. After phosphorylation at Y489, beta-adducin was translocated to the cell periphery, and colocalized with Fyn. These results suggest that Fyn phosphorylates and binds to beta-adducin at Y489, resulting in translocation of beta-adducin to the Fyn-enriched regions in the plasma membrane.
Gotoh
Hitoshi
H
Laboratory of Proteins Involved in Homeostatic Integration, Division of Integrated Protein Functions, Institute for Protein Research, Osaka University, Suita, Japan
Okumura
Nobuaki
N
Yagi
Takeshi
T
Okumura
Akiko
A
Shima
Takaki
T
Nagai
Katsuya
K
D000818:Animals; D019556:COS Cells; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002522:Chlorocebus aethiops; D007150:Immunohistochemistry; D051379:Mice; D018345:Mice, Knockout; D010766:Phosphorylation; D011485:Protein Binding; D021381:Protein Transport; D051076:Proto-Oncogene Proteins c-fyn / Q000235:genetics / Q000378:metabolism*; D011817:Rabbits; D015398:Signal Transduction; D014443:Tyrosine / Q000378:metabolism*; D000099291:Adducins
D002148:Calmodulin-Binding Proteins; D051076:Proto-Oncogene Proteins c-fyn; D014443:Tyrosine; D000099291:Adducins; C494960:Fyn protein, mouse