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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: J Neurochem. 2011 Oct 4;119(4):772–784. doi: 10.1111/j.1471-4159.2011.07468.x

Figure 2. The kinase/transition domains of mMyo3A and 3B autophosphorylate on serine and threonine residues.

Figure 2

A. Phosphorimages of the autophosphorylation of mMyo3A and 3B with time. B. Plot of the intensities of the phosphorylated bands shown in A versus time per µg of protein incubated. Incubations contained 5.6µg mMyo3A (closed circles) and 2.4µg mMyo3B (open circles). C. Phosphorimages of phosphorylated amino acids in the kinase/transition domains of mMyo3A and 3B following a 1hr incubation in vitro. Incubations contained 10µmol/l and 8µmol/l of mMyo3A and 3B, respectively. Phosphorylated amino acids were separated by two dimensional high voltage thin layer electrophoresis using a pH 1.9 buffer in the first dimension and a pH 3.5 buffer in the second dimension. Arrows indicate the directions of electrophoretic migration. White circles show the locations of the phosphoserine (S) and phosphothreonine (T) amino acid standards.