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PKC? is critical in AMPA receptor phosphorylation and synaptic incorporation during LTP.


ABSTRACT: Direct phosphorylation of GluA1 by PKC controls ?-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptor (AMPAR) incorporation into active synapses during long-term potentiation (LTP). Numerous signalling molecules that involved in AMPAR incorporation have been identified, but the specific PKC isoform(s) participating in GluA1 phosphorylation and the molecule triggering PKC activation remain largely unknown. Here, we report that the atypical isoform of PKC, PKC?, is a critical molecule that acts downstream of phosphatidylinositol 3-kinase (PI3K) and is essential for LTP expression. PKC? activation is required for both GluA1 phosphorylation and increased surface expression of AMPARs during LTP. Moreover, p62 interacts with both PKC? and GluA1 during LTP and may serve as a scaffolding protein to place PKC? in close proximity to facilitate GluA1 phosphorylation by PKC?. Thus, we conclude that PKC? is the critical signalling molecule responsible for GluA1-containing AMPAR phosphorylation and synaptic incorporation at activated synapses during LTP expression.

SUBMITTER: Ren SQ 

PROVIDER: S-EPMC3655466 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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PKCλ is critical in AMPA receptor phosphorylation and synaptic incorporation during LTP.

Ren Si-Qiang SQ   Yan Jing-Zhi JZ   Zhang Xiao-Yan XY   Bu Yun-Fei YF   Pan Wei-Wei WW   Yao Wen W   Tian Tian T   Lu Wei W  

The EMBO journal 20130319 10


Direct phosphorylation of GluA1 by PKC controls α-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptor (AMPAR) incorporation into active synapses during long-term potentiation (LTP). Numerous signalling molecules that involved in AMPAR incorporation have been identified, but the specific PKC isoform(s) participating in GluA1 phosphorylation and the molecule triggering PKC activation remain largely unknown. Here, we report that the atypical isoform of PKC, PKCλ, is a critical molec  ...[more]

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