MuSK Kinase Activity is Modulated By A Serine Phosphorylation Site in The Kinase Loop.
作者： B. Z. Camurdanoglu , C. Hrovat , G. Dürnberger , M. Madalinski , K. Mechtler
DOI: 10.1038/SREP33583
关键词: MAP kinase kinase kinase 、 Cyclin-dependent kinase 9 、 Kinase activity 、 MAP2K7 、 Chemistry 、 Agrin 、 Mitogen-activated protein kinase kinase 、 Cell biology 、 Cyclin-dependent kinase 5 、 Cyclin-dependent kinase 2
摘要: The neuromuscular junction (NMJ) forms when a motor neuron contacts muscle fibre. A reciprocal exchange of signals initiates cascade signalling events that result in pre- and postsynaptic differentiation. At the centre these stands specific kinase (MuSK). MuSK activation, activity subsequent downstream are crucial for NMJ formation as well maintenance. Therefore is tightly regulated to ensure proper development. We have identified novel serine phosphorylation site at position 751 increasingly phosphorylated upon agrin stimulation. S751 also tissue its depends on activity. phosphomimetic mutant increases response non-saturating concentrations . In addition, basal AChR cluster size increased. believe provides mechanism relief autoinhibition activation loop. Such lower could foster or stabilize especially during stages no low level present. Phosphorylation might therefore represent modulate prepatterning
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