CaMKII regulates proteasome phosphorylation and activity and promotes memory destabilization following retrieval

Jarome, Timothy J.; Ferrara, Nicole C.; Kwapis, Janine L.; Helmstetter, Fred J.

doi:10.1016/j.nlm.2016.01.001

Cited by 98 publications

(91 citation statements)

References 48 publications

(77 reference statements)

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“…While there is relatively little understanding of the neurochemical mechanisms of memory destabilization, several processes have been identified [101]. At the intracellular level, there appears to be a requirement for protein degradation at the proteasome [102, 103], protein phosphatase activity [104], CamKII [105] and nitric oxide [106, 107]. At the cell surface, there is a functional involvement of cholinergic [108] and dopaminergic receptors [109], at least for non-fear memory destabilization.…”

Section: The Reliability Of Reconsolidation Effectsmentioning

confidence: 99%

An Update on Memory Reconsolidation Updating

Lee

Nader

Schiller

2017

Trends in Cognitive Sciences

412

355

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The reactivation of a synaptically stored memory in the brain can make the memory transiently labile. During the time it takes for the memory to re-stabilize (reconsolidate), the memory can either be reduced by an amnesic agent or enhanced by memory enhancers. The change in memory expression is related to changes in the brain correlates of long-term memory. Many have suggested that such retrieval-induced plasticity is ideally placed to enable memories to be updated with new information. This hypothesis has been tested experimentally, with a translational perspective, by attempts to update maladaptive memories in order to reduce their problematic impact. Here, we review the progress on reconsolidation-update studies, highlighting their translational exploitation and addressing recent challenges to the reconsolidation field.

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Section: The Reliability Of Reconsolidation Effectsmentioning

confidence: 99%

An Update on Memory Reconsolidation Updating

Lee

Nader

Schiller

2017

Trends in Cognitive Sciences

412

355

View full text Add to dashboard Cite

show abstract

“…Some evidence suggests that a requirement for proteolysis in memory destabilization persists after memory retrieval, during the period of reconsolidation, and requires calcium/calmodulin-dependent kinase II (CaMKII) [68]. However, CaMKII is also requisite for extinction [69].…”

Section: Discrimination On the Basis Of Biochemical Mechanismsmentioning

confidence: 99%

New Learning and Unlearning: Strangers or Accomplices in Threat Memory Attenuation?

Clem

Schiller

2016

Trends in Neurosciences

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To achieve greatest efficacy, therapies for attenuating fear and anxiety should preclude the re-emergence of emotional responses. Of relevance to this aim, preclinical models of threat memory reduction are considered to engage one of two discrete neural processes: either establishment of a new behavioral response that competes with, and thereby temporarily interferes with expression of, an intact threat memory (new learning), or one which modifies and thereby disrupts an intact threat memory (unlearning). We contend that a strict dichotomy of new learning and unlearning does not provide a compelling explanation for current data. Instead, we suggest the evidence warrants consideration of alternative models that assume cooperation rather than competition between formation of new cellular traces and the modification of preexisting ones.

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“…Activated PKA phosphorylates Rpn6 on Ser14, whereas both PKA and CaMKII phosphorylate Rpt6 (58). Phosphorylation of Rpt6 by PKA and CaMKII initiates proteasome assembly by enhancing the direct association between Rpt6 and α2 (59, 60). In contrast, inhibition of CaMKII prevents the retrieval-induced increase in proteasome activity as well as the phosphorylation of Rpt6 on Ser120 in the amygdala (60).…”

Section: Regulation and Underlying Molecular Mechanisms Of Proteasomementioning

confidence: 99%

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

Im¹,

Chung²

2016

BMB Reports

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Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of NDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs. [BMB Reports 2016; 49(9): 459-473]

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CaMKII regulates proteasome phosphorylation and activity and promotes memory destabilization following retrieval

Cited by 98 publications

References 48 publications

An Update on Memory Reconsolidation Updating

An Update on Memory Reconsolidation Updating

New Learning and Unlearning: Strangers or Accomplices in Threat Memory Attenuation?

Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases

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