The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65

Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP rema...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 118; no. 9; pp. 1 - 10
Main Authors Chao-Hua, Jiang, Wei, Mengping, Zhang, Chen, Shi, Yun Stone
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 02.03.2021
Subjects
Animals
Biological Sciences
Embryo, Mammalian
Excitatory Postsynaptic Potentials - genetics
Female
Gene Expression Regulation
Genes, Reporter
Green Fluorescent Proteins - genetics
Green Fluorescent Proteins - metabolism
HEK293 Cells
Hippocampus - cytology
Hippocampus - metabolism
Humans
Long-Term Potentiation - genetics
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Male
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Mice
Primary Cell Culture
Protein Domains
Pyramidal Cells - cytology
Pyramidal Cells - metabolism
Receptors, AMPA - genetics
Receptors, AMPA - metabolism
Red Fluorescent Protein
Single-Cell Analysis
Synapses
LTP
AMPA receptors
GluA1
neuroplastin
amino-terminal domain
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Abstract Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.
AbstractList Long-term potentiation (LTP), the communication between neurons that is potentiated upon strong stimulus, is an important cellular mechanism underlying learning and memory. Mechanistically, LTP expression involves AMPA-type glutamate receptors insertion into synapses (initiation) and trapped at the synapses for an extended period of time (maintenance). Here, we show that the amino-terminal domain of GluA1, a subunit of AMPA receptors, selectively interacts with the adhesion protein Np65, and this interaction is required for the synaptic anchoring of AMPA receptors during LTP. Our study reveals a molecular mechanism underlying GluA1-dependent LTP maintenance. Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.
Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.
Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA receptor-dependent synaptic insertion of AMPA receptors (AMPARs). However, how AMPARs are recruited and anchored at the postsynaptic membrane during LTP remains largely unknown. In this study, using CRISPR/Cas9 to delete the endogenous AMPARs and replace them with the mutant forms in single neurons, we have found that the amino-terminal domain (ATD) of GluA1 is required for LTP maintenance. Moreover, we show that GluA1 ATD directly interacts with the cell adhesion molecule neuroplastin-65 (Np65). Neurons lacking Np65 exhibit severely impaired LTP maintenance, and Np65 deletion prevents GluA1 from rescuing LTP in AMPARs-deleted neurons. Thus, our study reveals an essential role for GluA1/Np65 binding in anchoring AMPARs at the postsynaptic membrane during LTP.
Author Zhang, Chen
Chao-Hua, Jiang
Shi, Yun Stone
Wei, Mengping
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AMPA receptors
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neuroplastin
amino-terminal domain
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1C.-H.J. and M.W. contributed equally to this work.
Edited by Roger A. Nicoll, University of California, San Francisco, CA, and approved January 22, 2021 (received for review September 13, 2020)
Author contributions: C.-H.J., C.Z., and Y.S.S. designed research; C.-H.J. and M.W. performed research; C.-H.J. and M.W. analyzed data; and C.-H.J. and Y.S.S. wrote the paper.
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Snippet Long-term potentiation (LTP) has long been considered as an important cellular mechanism for learning and memory. LTP expression involves NMDA...
Long-term potentiation (LTP), the communication between neurons that is potentiated upon strong stimulus, is an important cellular mechanism underlying...
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SubjectTerms Animals
Biological Sciences
Embryo, Mammalian
Excitatory Postsynaptic Potentials - genetics
Female
Gene Expression Regulation
Genes, Reporter
Green Fluorescent Proteins - genetics
Green Fluorescent Proteins - metabolism
HEK293 Cells
Hippocampus - cytology
Hippocampus - metabolism
Humans
Long-Term Potentiation - genetics
Luminescent Proteins - genetics
Luminescent Proteins - metabolism
Male
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Mice
Primary Cell Culture
Protein Domains
Pyramidal Cells - cytology
Pyramidal Cells - metabolism
Receptors, AMPA - genetics
Receptors, AMPA - metabolism
Red Fluorescent Protein
Single-Cell Analysis
Synapses
Title The amino-terminal domain of GluA1 mediates LTP maintenance via interaction with neuroplastin-65
URI https://www.jstor.org/stable/27027423
https://www.ncbi.nlm.nih.gov/pubmed/33627404
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