2018
DOI: 10.1038/s41467-018-04705-8
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Calmodulin shuttling mediates cytonuclear signaling to trigger experience-dependent transcription and memory

Abstract: Learning and memory depend on neuronal plasticity originating at the synapse and requiring nuclear gene expression to persist. However, how synapse-to-nucleus communication supports long-term plasticity and behavior has remained elusive. Among cytonuclear signaling proteins, γCaMKII stands out in its ability to rapidly shuttle Ca2+/CaM to the nucleus and thus activate CREB-dependent transcription. Here we show that elimination of γCaMKII prevents activity-dependent expression of key genes (BDNF, c-Fos, Arc), i… Show more

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Cited by 62 publications
(71 citation statements)
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“…It could be that in our experiments CAMK2D and CAMK2G are compensating for the absence of CAMK2A and CAMK2B. Indeed, evidence for a neuronal role for CAMK2G is emerging (Ma et al, 2014;Cohen et al, 2018;Proietti Onori et al, 2018). Together, it is clear that complete understanding of the precise role of presynaptic CAMK2 at the CA3-CA1 Schaffer collateral synapse is still lacking.…”
Section: Discussionmentioning
confidence: 55%
“…It could be that in our experiments CAMK2D and CAMK2G are compensating for the absence of CAMK2A and CAMK2B. Indeed, evidence for a neuronal role for CAMK2G is emerging (Ma et al, 2014;Cohen et al, 2018;Proietti Onori et al, 2018). Together, it is clear that complete understanding of the precise role of presynaptic CAMK2 at the CA3-CA1 Schaffer collateral synapse is still lacking.…”
Section: Discussionmentioning
confidence: 55%
“…Calmodulin (CaM) interacts with CTD of GluN2A subunit in a calcium-dependent manner at the 875-1029 domain, through interaction with a tryptophan residue (1014), which is critical for protein-protein interaction [103]. Ca 2+ /Calmodulin complexes can be also considered as a synapse-to-nucleus messengers of the γCaMKII and γCaMKI signaling, regulating gene expression and cognitive functions [104][105][106].…”
Section: Other Proteinsmentioning
confidence: 99%
“…These CTD mutations might disrupt CREB signaling by interfering with the formation of the local Ca 2+ nanodomain and/or with the conformational changes in the LTCC (Li et al, 2016). The CTD of CaV1.3, but not CaV1.2, was shown to interact with the PDZ domains of Shank1 or Shank3 (Zhang et al, 2005) (Cohen et al, 2018, Ma et al, 2014. Since trans-autophosphorylation between two separate holoenzymes is highly inefficient in solution (Hanson et al, 1994), another hypothesis is that the two CaMKII-binding sites within the same LTCC complex might bring two holoenzymes in sufficiently close proximity to overcome this biochemical barrier.…”
Section: Role Of Camkii-shank3-cav13 Complex In Ltcc-creb Signalingmentioning
confidence: 99%
“…Recent studies have shown that the initiation of LTCC-dependent E-T coupling requires the recruitment of multiple CaMKII holoenzymes to a nanodomain close to LTCCs (Ma et al, 2014, Wheeler et al, 2008. Moreover, a CaMKII mutation linked to intellectual disability disrupts neuronal E-T coupling (Cohen et al, 2018). However, the molecular mechanisms underlying the organization and function of this LTCC nanodomain remain incompletely understood.…”
Section: Introductionmentioning
confidence: 99%