Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic overexcitation.

Nature neuroscience | Oct 29, 2010

Trafficking of AMPA receptors (AMPARs) is important for many forms of synaptic plasticity. However, the link between activity and resulting synaptic alterations is not fully understood. We identified a direct interaction between N-ethylmaleimide-sensitive fusion protein (NSF), an ATPase involved in membrane fusion events and stabilization of surface AMPARs, and Polo-like kinase- 2 (Plk2), an activity-inducible kinase that homeostatically decreases excitatory synapse number and strength. Plk2 disrupted the interaction of NSF with the GluA2 subunit of AMPARs, promoting extensive loss of surface GluA2 in rat hippocampal neurons, greater association of GluA2 with adaptor proteins PICK1 and GRIP1, and decreased synaptic AMPAR current. Plk2 engagement of NSF, but not Plk2 kinase activity, was required for this mechanism and occurred through a motif in the Plk2 protein that was independent of the canonical polo box interaction sites. These data reveal that heightened synaptic activity, acting through Plk2, leads to homeostatic decreases in surface AMPAR expression via the direct dissociation of NSF from GluA2.

Pubmed ID: 20802490 RIS Download

Mesh terms: Adenosine Triphosphate | Amino Acid Motifs | Animals | Carrier Proteins | Cells, Cultured | Cercopithecus aethiops | Embryo, Mammalian | Endocytosis | GABA Antagonists | Gene Expression Regulation | Green Fluorescent Proteins | Hippocampus | Homeostasis | Humans | Immunoprecipitation | Microscopy, Confocal | N-Ethylmaleimide-Sensitive Proteins | Nerve Tissue Proteins | Neurons | Nuclear Proteins | Picrotoxin | Protein Binding | Protein Transport | Protein-Serine-Threonine Kinases | RNA Interference | Rats | Receptors, AMPA | Synapses | Time Factors | Transfection

Research resources used in this publication

Research tools detected in this publication

Data used in this publication

None found

Associated grants

  • Agency: NINDS NIH HHS, Id: F31 NS061467
  • Agency: NINDS NIH HHS, Id: F31 NS061467-03
  • Agency: NINDS NIH HHS, Id: R01 NS048085-05
  • Agency: NCI NIH HHS, Id: P30CA051008
  • Agency: NINDS NIH HHS, Id: R01 NS048085
  • Agency: NCI NIH HHS, Id: P30 CA051008
  • Agency: NINDS NIH HHS, Id: NS048085
  • Agency: NINDS NIH HHS, Id: F31NS061467

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

This is a list of tools and resources that we have found mentioned in this publication.


MetaMorph Microscopy Automation and Image Analysis Software

Software tool for automated microscope acquisition, device control, and image analysis. Used for integrating dissimilar fluorescent microscope hardware and peripherals into a single custom workstation, while providing all the tools needed to perform analysis of acquired images. Offers user friendly application modules for analysis such as cell signaling, cell counting, and protein expression.

tool

View all literature mentions

pClamp

Software suite for electrophysiology data acquisition and analysis by Molecular Devices. Used for the control and recording of voltage clamp, current clamp, and patch clamp experiments. The software suite consists of Clampex 11 Software for data acquisition, AxoScope 11 Software for background recording, Clampfit 11 Software for data analysis, and optional Clampfit Advanced Analysis Module for sophisticated and streamlined analysis.

tool

View all literature mentions