Protein Phosphotase 1α Reverses UNC-51 Phosphorylations of Both Actins and Tubulins and a New Model of UNC-51-Inducing Axon Formation
Because UNC-51 can promote depolymerization-dynamics of microtubules (being submitted to Science Signaling), and Protein phosphotase 1α has microtubule-stabilizing functions (Liao, et al., 1998), we showed that protein phosphotase 1α efficiently dephosphorylated UNC-51 phosphorylations of actins and tubulins, and hypothesized a new model of UNC-51-inducing axon formation.
Keywordskinase UNC-51 tubulin actin depolymerization PP1 axon formation model
We are very thankful to Drs. K. Hayashi and T. Tahira, T. Tani, K. Nakayama, A. Yamanaka, K. Mizuno, K. Tawada, Y. Emoto, H. Arata, K. Katayama, Y. Fujiki, Y. Fukumaki, M. Kimura, S. Osaki, I. Ito and Y. Kato for kindly providing pCAGGS vector, COS cells, HeLa cells, HEK293T cells, pUcD2SRαMCS, Beckman Optima centrifuge, French press, the computer system, kind discussion, advice, help and encouragement. We express sincere gratitude to all members of both laboratories for their help and encouragement.