Proteomics

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Neuroligin 2 Governs Synaptic Morphology and Function Through RACK1-Cofilin Signaling in Drosophila


ABSTRACT: Neuroligins are transmembrane cell adhesion proteins well-known for their genetic links to autism spectrum disorders. Neuroligins can function by regulating the actin cytoskeleton, however the factors and mechanisms involved are still largely unknown. Here, using the Drosophila neuromuscular junction as a model, we reveal that F-Actin assembly at the Drosophila NMJ is controlled through Cofilin signaling mediated by an interaction between DNlg2 and RACK1, factors not previously known to work together. The deletion of DNlg2 displays disrupted RACK1-Cofilin signaling pathway with diminished actin cytoskeleton proteo-stasis at the terminal of the NMJ, aberrant NMJ structure, reduced synaptic transmission, and abnormal locomotion at the third-instar larval stage. Overexpression of wildtype and activated Cofilin in muscles are sufficient to rescue the morphological and physiological defects in dnlg2 mutants, while inactivated Cofilin is not. Since the DNlg2 paralog DNlg1 is known to regulate F-actin assembly mainly via a specific interaction with WAVE complex, our present work suggests that the orchestration of F-actin by Neuroligins is a highly dynamic and complex process critical for neural connectivity.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Whole Body

SUBMITTER: Yichen Sun  

LAB HEAD: Wei Xie

PROVIDER: PXD045754 | Pride | 2023-10-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
DNlg2Cterminal1.dat Other
DNlg2Cterminal1.raw Raw
DNlg2Cterminal2.dat Other
DNlg2Cterminal2.raw Raw
DNlg2Cterminal3.dat Other
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