ArticleProceedings of the National Academy of Sciences of the United States of America2014
GRIP1 interlinks N-cadherin and AMPA receptors at vesicles to promote combined cargo transport into dendrites.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 71 citations in OpenAlex.
- SNX6-mediated subunit-specific secretory trafficking of AMPA receptors regulates synaptic function and plasticity.Communications biology · 2025Article
- Dynein-driven regulation of postsynaptic membrane architecture and synaptic function.Journal of cell science · 2025Article
- Amyloid-β-Driven Synaptic Deficits Are Mediated by Synaptic Removal of GluA3-Containing AMPA Receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Cellular junction dynamics and Alzheimer's disease: a comprehensive review.Molecular biology reports · 2024Review
- Plk2 promotes synaptic destabilization through disruption of N-cadherin adhesion complexes during homeostatic adaptation to hyperexcitation.Journal of neurochemistry · 2023Article
- Tubb3 expression levels are sensitive to neuronal activity changes and determine microtubule growth and kinesin-mediated transport.Cellular and molecular life sciences : CMLS · 2022Article
- Familial ALS-associatedOpen biology · 2022Article
- The needs of a synapse-How local organelles serve synaptic proteostasis.The EMBO journal · 2022Review
- KIF2C regulates synaptic plasticity and cognition in mice through dynamic microtubule depolymerization.eLife · 2022Article
- Scaffold Protein Lnx1 Stabilizes EphB Receptor Kinases for Synaptogenesis.Frontiers in molecular neuroscience · 2022Article
- Glutamate receptor-interacting protein 1 in D1- and D2-dopamine receptor-expressing medium spiny neurons differentially regulates cocaine acquisition, reinstatement, and associated spine plasticity.Frontiers in cellular neuroscience · 2022Article
- Decreased Reactive Oxygen Species Signaling Alters Glutamate Receptor Transport to Synapses inmicroPublication biology · 2022Article
- KIF13A drives AMPA receptor synaptic delivery for long-term potentiation via endosomal remodeling.The Journal of cell biology · 2021Article
- Article
- EphrinB2 and GRIP1 stabilize mushroom spines during denervation-induced homeostatic plasticity.Cell reports · 2021Article
- Mammalian Neuronal mRNA Transport Complexes: The Few Knowns and the Many Unknowns.Frontiers in integrative neuroscience · 2021Review
- Review
- Microtubules and motor proteins support zebrafish neuronal migration by directing cargo.The Journal of cell biology · 2020Article
- Molecular and Cellular Mechanisms Affected in ALS.Journal of personalized medicine · 2020Review
- Spastin depletion increases tubulin polyglutamylation and impairs kinesin-mediated neuronal transport, leading to working and associative memory deficits.PLoS biology · 2020Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GluA2 subunit of AMPA-type glutamate receptors (AMPARs) regulates excitatory synaptic transmission in neurons. In addition, the transsynaptic cell adhesion molecule N-cadherin controls excitatory synapse function and stabilizes dendritic spine structures. At postsynaptic membranes, GluA2 physically binds N-cadherin, underlying spine growth and synaptic modulation. We report that N-cadherin binds to PSD-95/SAP90/DLG/ZO-1 (PDZ) domain 2 of the glutamate receptor interacting protein 1 (GRIP1) through its intracellular C terminus. N-cadherin and GluA2-containing AMPARs are presorted to identical transport vesicles for dendrite delivery, and live imaging reveals cotransport of both proteins. The kinesin KIF5 powers GluA2/N-cadherin codelivery by using GRIP1 as a multilink interface. Notably, GluA2 and N-cadherin use different PDZ domains on GRIP1 to simultaneously bind the transport complex, and interference with either binding motif impairs the turnover of both synaptic cargoes. Depolymerization of microtubules, deletion of the KIF5 motor domain, or specific blockade of AMPAR exocytosis affects delivery of GluA2/N-cadherin vesicles. At the functional level, interference with this cotransport reduces the number of spine protrusions and excitatory synapses. Our data suggest the concept that the multi-PDZ-domain adaptor protein GRIP1 can act as a scaffold at trafficking vesicles in the combined delivery of AMPARs and N-cadherin into dendrites.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.