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- W2041102021 abstract "Neural activity regulates dendrite and synapse development, but the underlying molecular mechanisms are unclear. Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an important sensor of synaptic activity, and the scaffold protein liprinalpha1 is involved in pre- and postsynaptic maturation. Here we show that synaptic activity can suppress liprinalpha1 protein level by two pathways: CaMKII-mediated degradation and the ubiquitin-proteasome system. In hippocampal neurons, liprinalpha1 mutants that are immune to CaMKII degradation impair dendrite arborization, reduce spine and synapse number, and inhibit dendritic targeting of receptor tyrosine phosphatase LAR, which is important for dendrite development. Thus, regulated degradation of liprinalpha1 is important for proper LAR receptor distribution, and could provide a mechanism for localized control of dendrite and synapse morphogenesis by activity and CaMKII." @default.
- W2041102021 created "2016-06-24" @default.
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- W2041102021 date "2007-04-01" @default.
- W2041102021 modified "2023-09-24" @default.
- W2041102021 title "Liprinα1 Degradation by Calcium/Calmodulin-Dependent Protein Kinase II Regulates LAR Receptor Tyrosine Phosphatase Distribution and Dendrite Development" @default.
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- W2041102021 doi "https://doi.org/10.1016/j.devcel.2007.02.006" @default.
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