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The postsynaptic architecture of excitatory synapses: a more quantitative view.
The structures of some intact PSD proteins, as well as the spatial arrangement of several proteins within the PSD, have been determined at low resolution by electron microscopy, and a more quantitative and geometrically realistic view of PSD architecture is emerging.
Visualization of Microtubule Growth in Cultured Neurons via the Use of EB3-GFP (End-Binding Protein 3-Green Fluorescent Protein)
It is proposed that similar mechanisms underlie the specific association of CLIPs and EB1-related proteins with the ends of growing microtubules in non-neuronal and neuronal cells and contributes to the formation of the microtubule network in all neuronal compartments.
CLASPs Are CLIP-115 and -170 Associating Proteins Involved in the Regional Regulation of Microtubule Dynamics in Motile Fibroblasts
STIM1 Is a MT-Plus-End-Tracking Protein Involved in Remodeling of the ER
Actin in dendritic spines: connecting dynamics to function
Emerging evidence suggests that most signaling pathways linking synaptic activity to spine morphology influence local actin dynamics, and specific mechanisms of actin regulation are integral to the formation, maturation, and plasticity of dendritic spines and to learning and memory.
Control of Dendritic Arborization by the Phosphoinositide-3′-Kinase–Akt–Mammalian Target of Rapamycin Pathway
- J. Jaworski, S. Spangler, D.P. Seeburg, C. Hoogenraad, M. Sheng
- BiologyThe Journal of Neuroscience
- 7 December 2005
It is shown that the phosphoinositide-3′ kinase (PI3K)–Akt–mammalian target of rapamycin (mTOR) signaling pathway promotes the growth and branching of dendrites in cultured hippocampal neurons.
Bicaudal-D regulates COPI-independent Golgi–ER transport by recruiting the dynein–dynactin motor complex
It is suggested that coordinated action between Rab6a, BICD and the dynein–dynactin complex controls COPI-independent Golgi–ER transport.
Dynamic Microtubules Regulate Dendritic Spine Morphology and Synaptic Plasticity
Rab6 regulates transport and targeting of exocytotic carriers.
Motor Neuron Disease-Associated Mutant Vesicle-Associated Membrane Protein-Associated Protein (VAP) B Recruits Wild-Type VAPs into Endoplasmic Reticulum-Derived Tubular Aggregates
- E. Teuling, Suaad Ahmed, C. Hoogenraad
- Biology, ChemistryThe Journal of Neuroscience
- 5 September 2007
The data support a model in which reduced levels of VAP family proteins result in decreased ER anchoring of lipid-binding proteins and cause motor neuron degeneration.