Journal: The Journal of Cell Biology

Article Title: α-Syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner

doi: 10.1083/jcb.200412008

Figure Lengend Snippet: ARMS and α-syntrophin enhanced the EphA4-induced Jak/Stat activation. (A) COS7 cells were transfected with EphA4, EphA4 KD mutant, or ARMS, and cell lysate was immunoblotted with antibodies against phosphorylated Tyr 1007/1008 of mouse Jak2, Tyr 1054/1055 of human Tyk2, Tyr 701 of Stat1, and Thr 202 /Tyr 204 of ERK1/2. p-Tyr; phosphorylated Tyr. (B) Quantification of the Western blots. y axis represents the fold change of tyrosine phosphorylation. n = 3; *, P < 0.05; **, P < 0.005. (C) COS7 cells were transfected with EphA4, ARMS, α-syntrophin, or α-syntrophin mPDZ, and cell lysate was immunoblotted with antibodies against phosphorylated Tyr 1007/1008 of mouse Jak2, Tyr 1054/1055 of human Tyk2, Tyr 701 of Stat1, and Thr 202 /Tyr 204 of ERK1/2. (D) Quantification of the Western blots. n = 3; *, P < 0.05; **, P < 0.005. Error bars represent the SEM.

Article Snippet: Antibodies against phosphotyrosine residues, phosphorylated Tyr 701 Stat1, Tyr 1004/1005 Tyk2, and threonine/tyrosine-phosphorylated extracellular signal–regulated kinase (ERK) 1/2 were purchased from Cell Signaling, Inc., and antibody against phosphorylated Tyr 1007/1008 Jak2 was purchased from Upstate Biotechnology.

Techniques: Activation Assay, Transfection, Mutagenesis, Western Blot