Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity

Q Wu, M Sun, LP Bernard, H Zhang - Journal of Biological Chemistry, 2017 - ASBMB
Postsynaptic density 95 (PSD-95) is a major synaptic scaffolding protein that plays a key role
in bidirectional synaptic plasticity, which is a process important for learning and memory. It is …

Activity-independent regulation of dendrite patterning by postsynaptic density protein PSD-95

EI Charych, BF Akum, JS Goldberg… - Journal of …, 2006 - Soc Neuroscience
Dendritic morphology determines many aspects of neuronal function, including action
potential propagation and information processing. However, the question remains as to how …

S-nitrosylation and S-palmitoylation reciprocally regulate synaptic targeting of PSD-95

GPH Ho, B Selvakumar, J Mukai, LD Hester, Y Wang… - Neuron, 2011 - cell.com
PSD-95, a principal scaffolding component of the postsynaptic density, is targeted to
synapses by palmitoylation, where it couples NMDA receptor stimulation to production of …

PDZ domain proteins of synapses

E Kim, M Sheng - Nature Reviews Neuroscience, 2004 - nature.com
PDZ domains are protein-interaction domains that are often found in multi-domain
scaffolding proteins. PDZ-containing scaffolds assemble specific proteins into large …

[HTML][HTML] Clustering membrane proteins: It's all coming together with the PSD-95/SAP90 protein family

SN Gomperts - Cell, 1996 - cell.com
Neurons differentially localize and cluster membrane proteins. Spatial localization and
clustering of ion channels and neurotransmitter receptors are necessary for neurons to fire …

Site-specific phosphorylation of PSD-95 PDZ domains reveals fine-tuned regulation of protein–protein interactions

SW Pedersen, L Albertsen, GE Moran… - ACS chemical …, 2017 - ACS Publications
The postsynaptic density protein of 95 kDa (PSD-95) is a key scaffolding protein that controls
signaling at synapses in the brain through interactions of its PDZ domains with the C-termini …

[HTML][HTML] Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions

T Nakagawa, K Futai, HA Lashuel, I Lo, K Okamoto… - Neuron, 2004 - cell.com
Single-particle electron microscopy (EM) combined with biochemical measurements
revealed the molecular shape of SAP97 and a monomer-dimer transition that depended on …

Local palmitoylation cycles define activity-regulated postsynaptic subdomains

Y Fukata, A Dimitrov, G Boncompain… - Journal of Cell …, 2013 - rupress.org
Distinct PSD-95 clusters are primary landmarks of postsynaptic densities (PSDs), which are
specialized membrane regions for synapses. However, the mechanism that defines the …

PSD-95 is required for activity-driven synapse stabilization

I Ehrlich, M Klein, S Rumpel… - Proceedings of the …, 2007 - National Acad Sciences
The activity-dependent regulation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid
(AMPA)-type glutamate receptors and the stabilization of synapses are critical to synaptic …

Cyclin-dependent kinase 5 phosphorylates the N-terminal domain of the postsynaptic density protein PSD-95 in neurons

MA Morabito, M Sheng, LH Tsai - Journal of Neuroscience, 2004 - Soc Neuroscience
PSD-95 (postsynaptic density 95) is a postsynaptic scaffolding protein that links NMDA
receptors to the cytoskeleton and signaling molecules. The N-terminal domain of PSD-95 is …