Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction

Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila...

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Bibliographic Details
Published in:Biology open 2014-12, Vol.3 (12), p.1196-1206
Main Authors: Wang, Simon Ji Hau, Tsai, Amy, Wang, Mannan, Yoo, SooHyun, Kim, Hae-Yoon, Yoo, Byoungjoo, Chui, Vincent, Kisiel, Marta, Stewart, Bryan, Parkhouse, Wade, Harden, Nicholas, Krieger, Charles
Format: Article
Language:English
Subjects:
Actin
Adducin
Alanine
Ca2+/calmodulin-dependent protein kinase II
Cytoskeleton
Dlg
Drosophila
Fruit flies
Homology
Hts
Insects
Isoforms
Kinases
MARCKS protein
Muscles
Neuromuscular junction
Neuromuscular junctions
Phosphatidylinositol 4,5-diphosphate
Phosphorylation
PIP2
Plasticity
Protein kinase C
Proteinase-activated receptor 1
Proteins
Spectrin
Synaptic plasticity
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Summary:Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.
ISSN:2046-6390
2046-6390
DOI:10.1242/bio.20148342