Autophosphorylated CaMKIIα Acts as a Scaffold to Recruit Proteasomes to Dendritic Spines
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Autophosphorylated CaMKIIα Acts as a Scaffold to Recruit Proteasomes to Dendritic Spines
The molecular mechanisms regulating the ubiquitin proteasome system (UPS) at synapses are poorly understood. We report that CaMKIIalpha-an abundant postsynaptic protein kinase-mediates the activity-dependent recruitment of proteasomes to dendritic spines in hippocampal neurons. CaMKIIalpha is biochemically associated with proteasomes in the brain. CaMKIIalpha translocation to synapses is requir...
متن کاملCaMKIIβ Functions As an F-Actin Targeting Module that Localizes CaMKIIα/β Heterooligomers to Dendritic Spines
of CaMKIIa, the regulation of different CaMKII isoforms Ca/calmodulin-dependent protein kinase II (CaMKII) by Ca/CaM and autophosphorylation is similar overall is a serine/threonine protein kinase that regulates (Miller and Kennedy, 1985; GuptaRoy and Griffith, 1996; long-term potentiation and other forms of neuronal plasDe Koninck and Schulman, 1998). Despite these similariticity. Functional d...
متن کاملEditorial: Dendritic spines: from shape to function†
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متن کاملDendritic Spines
Dendritic spines are important sites of excitatory synaptic transmission and changes in the strength of these synapses are likely to underlie important higher brain functions such as learning and memory. Spines form biochemical compartments for isolating reactions that occur at one synapse from those at other synapses thereby providing a possible way to ensure the specificity of connections bet...
متن کاملDendritic Spines
What are they? Dendritic spines are small protrusions that emerge from the dendrites of neurons (Figure 1). Most excitatory synapses in the brain are found on spine heads. Typically, a spine consists of a bulbous head, volume 0.001–1 μm3, at the end of a thin spine neck, diameter around 0.1 μm. A 100 μm length dendrite can contain several hundred spines. The human cerebral cortex is thought to ...
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ژورنال
عنوان ژورنال: Cell
سال: 2010
ISSN: 0092-8674
DOI: 10.1016/j.cell.2010.01.024