TY - JOUR
T1 - Nemo kinase interacts with Mad to coordinate synaptic growth at the Drosophila neuromuscular junction
AU - Merino, Carlos
AU - Penney, Jay
AU - González, Miranda
AU - Tsurudome, Kazuya
AU - Moujahidine, Myriam
AU - O'Connor, Michael B.
AU - Verheyen, Esther M.
AU - Haghighi, Pejmun
PY - 2009/5/18
Y1 - 2009/5/18
N2 - Bone morphogenic protein (BMP) signaling is essential for the coordinated assembly of the synapse, but we know little about how BMP signaling is modulated in neurons. Our findings indicate that the Nemo (Nmo) kinase modulates BMP signaling in motor neurons. nmo mutants show synaptic structural defects at the Drosophila melanogaster larval neuromuscular junction, and providing Nmo in motor neurons rescues these defects. We show that Nmo and the BMP transcription factor Mad can be coimmunoprecipitated and find a genetic interaction between nmo and Mad mutants. Moreover, we demonstrate that Nmo is required for normal distribution and accumulation of phosphorylated Mad in motor neurons. Finally, our results indicate that Nmo phosphorylation of Mad at its N terminus, distinct from the BMP phosphorylation site, is required for normal function of Mad. Based on our findings, we propose a model in which phosphorylation of Mad by Nmo ensures normal accumulation and distribution of Mad and thereby fine tunes BMP signaling in motor neurons.
AB - Bone morphogenic protein (BMP) signaling is essential for the coordinated assembly of the synapse, but we know little about how BMP signaling is modulated in neurons. Our findings indicate that the Nemo (Nmo) kinase modulates BMP signaling in motor neurons. nmo mutants show synaptic structural defects at the Drosophila melanogaster larval neuromuscular junction, and providing Nmo in motor neurons rescues these defects. We show that Nmo and the BMP transcription factor Mad can be coimmunoprecipitated and find a genetic interaction between nmo and Mad mutants. Moreover, we demonstrate that Nmo is required for normal distribution and accumulation of phosphorylated Mad in motor neurons. Finally, our results indicate that Nmo phosphorylation of Mad at its N terminus, distinct from the BMP phosphorylation site, is required for normal function of Mad. Based on our findings, we propose a model in which phosphorylation of Mad by Nmo ensures normal accumulation and distribution of Mad and thereby fine tunes BMP signaling in motor neurons.
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U2 - 10.1083/jcb.200809127
DO - 10.1083/jcb.200809127
M3 - Article
C2 - 19451277
AN - SCOPUS:66149158431
SN - 0021-9525
VL - 185
SP - 713
EP - 725
JO - Journal of Cell Biology
JF - Journal of Cell Biology
IS - 4
ER -