THESIS
2019
xiii, 72 pages : illustrations (some color) ; 30 cm
Abstract
Cell adhesion molecules (CAMs) are key molecules involved in synaptogenesis by
regulating neuron initiation contact, synapse formation and maturation. Asymmetric
Neurexin-Neuroligin partner is extensively investigated among CAMs, not only because
of its function in synaptogenesis, but also because of its specific mutation in human
Autism spectrum disorders. Neuroligin2 (NLGN2), a member of Neuroligin families,
exclusively expresses at the inhibitory synapses and regulates the formation of inhibitory
synapses. Although the importance of NLGN2 in inhibitory synapse formation is
highlighted in several studies, the function of NLGN2 in regulating protein trafficking is
poorly unknown. To better understand the function of NLGN2, we performed
co-immunoprecipitation mass spectrometry...[
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Cell adhesion molecules (CAMs) are key molecules involved in synaptogenesis by
regulating neuron initiation contact, synapse formation and maturation. Asymmetric
Neurexin-Neuroligin partner is extensively investigated among CAMs, not only because
of its function in synaptogenesis, but also because of its specific mutation in human
Autism spectrum disorders. Neuroligin2 (NLGN2), a member of Neuroligin families,
exclusively expresses at the inhibitory synapses and regulates the formation of inhibitory
synapses. Although the importance of NLGN2 in inhibitory synapse formation is
highlighted in several studies, the function of NLGN2 in regulating protein trafficking is
poorly unknown. To better understand the function of NLGN2, we performed
co-immunoprecipitation mass spectrometry and found CLU as potential candidate of
NLGN2 binding partner. We firstly performed in vitro co-immunoprecipitation and
verified that NLGN2 could interact with the mature form of CLU. When co-expressed
this protein and NLGN2 in HEK293T cells, they co-localized and formed new puncta at
Golgi sites. In addition, NLGN2 affected CLU protein levels in vitro and in vivo, which
mediated the process of cell autophagy. Further studies to investigate the function of their
interaction may provide new understanding for NLGN2 in regulating protein secretion.
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