One‐Trial <i>In Vitro</i> Conditioning of <i>Hermissenda</i> Regulates Phosphorylation of Ser‐122 of Csp24

Crow, Terry; Xue-Bian, Juan-Juan

doi:10.1196/annals.1415.012

Cited by 5 publications

(8 citation statements)

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“…The present results compliment our previous study showing that enhanced excitability detected after one-trial in vitro conditioning is blocked by antisense oligonucleotide-mediated downregulation of Csp24 (Crow et al 2003). Previous work has shown that Csp24 is phosphorylated by one-trial in vitro conditioning and multi-trial Pavlovian conditioning (Crow et al 1999, 2003; Crow and Xue-Bian 2000, 2003, 2007, 2010; Redell et al 2007). The depolarized shift in the activation curve of I A proposed to contribute to one-trial conditioning-dependent enhanced excitability is blocked by preincubation of sensory neurons with Csp antisense oligonucleotide (Yamoah et al 2005).…”

Section: Discussionmentioning

confidence: 99%

“…One-trial in vitro conditioning consists of pairing the CS (Light) with the application of 5-HT to the isolated nervous system. In vitro conditioning has been shown to produce multiple stages of time-dependent enhanced excitability in sensory neurons (photoreceptors), synaptic facilitation of the monosynaptic connection between sensory neurons and interneurons, and changes in protein phosphorylation (Crow & Forrester 1991,1993; Crow & Siddiqi 1997; Crow & Xue-Bian 2000, 2002, 2007, 2010; Crow et al 1996,1997,1998,1999, 2003; Yamoah et al 2005; Redell et al 2007). …”

Section: Methodsmentioning

confidence: 99%

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Proteomic analysis of short- and intermediate-term memory in Hermissenda

Crow¹,

Xue-Bian²

2011

Neuroscience

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Changes in cellular and synaptic plasticity related to learning and memory are accompanied by both up-regulation and down-regulation of the expression levels of proteins. Both de novo protein synthesis and post-translational modification of existing proteins have been proposed to support the induction and maintenance of memory underlying learning. However, little is known regarding the identity of proteins regulated by learning that are associated with the early stages supporting the formation of memory over-time. In this study we have examined changes in protein abundance at two different times following one-trial in vitro conditioning of Hermissenda using two-dimensional difference gel electrophoresis (2D-DIGE), quantification of differences in protein abundance between conditioned and unpaired controls, and protein identification with tandem mass spectrometry. Significant regulation of protein abundance following one-trial in vitro conditioning was detected 30 min and 3 hr post-conditioning. Proteins were identified that exhibited statistically significant increased or decreased abundance at both 30 min and 3 hr post-conditioning. Proteins were also identified that exhibited a significant increase in abundance only at 30 min, or only at 3 hr post-conditioning. A few proteins were identified that expressed a significant decrease in abundance detected at both 30 min and 3 hr post-conditioning, or a significant decrease in abundance only at 3 hr post-conditioning. The proteomic analysis indicates that proteins involved in diverse cellular functions such as translational regulation, cell signaling, cytoskeletal regulation, metabolic activity, and protein degradation contribute to the formation of memory produced by one-trial in vitro conditioning. These findings support the view that changes in protein abundance over-time following one-trial in vitro conditioning involve dynamic and complex interactions of the proteome.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Proteomic analysis of short- and intermediate-term memory in Hermissenda

Crow¹,

Xue-Bian²

2011

Neuroscience

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“…Protein kinase C influenced co-precipitation of Csp24 with actin is regulated by one-trial in vitro conditioning and recombinant Csp24 sequesters G-actin in vitro (Redell et al, 2007). The phosphorylation of Ser-122, but not Ser-49 of Csp24 is produced by conditioning procedures that result in intermediate-term and long-term intrinsic enhanced excitability, but not after procedures that result in short-term changes in excitability of sensory neurons (Crow et al, 1999; Crow and Xue-Bian, 2000, 2007). Moreover, treatment with a Csp antisense oligonucleotide (ON) before one-trial conditioning blocks intermediate-term enhanced excitability, without affecting the induction of short-term enhanced excitability (Crow et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of post-translational modifications in conditioned Hermissenda

Crow¹,

Xue-Bian²

2010

Neuroscience

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Post-translational modifications of proteins are a major determinant of biological function. Phosphorylation of proteins involved in signal transduction contributes to the induction and maintenance of several examples of cellular and synaptic plasticity. In this study we have identified phosphoproteins regulated by Pavlovian conditioning in lysates of Hermissenda nervous systems using 2DE in conjunction with 32 P labeling, fluorescence based phosphoprotein in-gel staining, and mass spectrometry. Modification of protein phosphorylation regulated by conditioning was first assessed by densitometric analysis of 32 P labeled proteins resolved by 2DE from lysates of conditioned and pseudorandom control nervous systems. An independent assessment of phosphorylation regulated by conditioning was obtained from an examination of 2D gels stained with Pro-Q Diamond phosphoprotein dye. Mass spectrometric analysis of protein digests from phosphoprotein stained analytical gels or Coomassie blue stained preparative gels provided for the identification of phosphoproteins that exhibited statistically significant increased phosphorylation in conditioned groups as compared to pseudorandom controls. A previously identified cytoskeletal related protein, Csp24, involved in intermediate-term memory exhibited significantly increased phosphorylation detected 24 hrs post-conditioning. Our results show that proteins involved in diverse cellular functions such as transcriptional regulation, cell signaling, cytoskeletal regulation, metabolic activity, and protein degradation contribute to long-term post-translational modifications associated with Pavlovian conditioning. Keywordsβ-thymosin repeat protein; Hermissenda; cytoskeletal proteins; Pavlovian conditioning; posttranslational modificationPost-translational modifications that change the properties of proteins are of major importance for biological function. For example, a number of biological events such as signal transduction, transcriptional regulation, control of enzyme activity, and cell division are regulated by the phosphorylation of proteins (for reviews see Hunter and Karin, 1992;Johnson and Vaillancourt, 1994;Hunter, 1995;Karin and Hunter, 1995;Johnston and O'Reilly, 1996;Mann and Jensen, 2003). In addition, phosphorylation is now recognized as important in the induction Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access Author ManuscriptNeuroscience. Author manuscript; available in PMC 2011 February 17. and maintenance of cellular and synaptic plasticity (for example see Neary et al., 1981;Sweatt and Kandel, 1989;Cr...

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“…Two phosphorylation sites on Csp24 have been recently identified using electrospray mass spectrometry. One-trial in vitro conditioning regulates the phosphorylation of Ser122, but not Ser49 of Csp24 [11]. The potential regulation of the interaction between 14-3-3 protein and Csp24 by phosphorylation was assessed by the analysis of 5-HT-dependent phosphorylation of Csp24 co-precipitates generated by immunoprecipitated 14-3-3 protein.…”

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confidence: 99%

“…The nervous systems were lysed and immunoprecipitation experiments were conducted with anti 14-3-3 antibody. The immmunoprecipitates from experimental and control groups were blotted and probed with phosphospecific antibodies directed to Ser122 or Ser49 as previously described [11]. Following densitometric scanning the membranes were stripped and reprobed with anti-Csp24 antibody and scanned to provide assessment of total Csp24 levels.…”

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confidence: 99%

14-3-3 proteins interact with the β-thymosin repeat protein Csp24

Crow¹,

Xue-Bian²,

Neary

2007

Neuroscience Letters

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Conditioned stimulus pathway protein 24 (Csp24) is a beta-thymosin-like protein that is homologous to other members of the family of beta-thymosin repeat proteins that contain multiple actin binding domains. Actin co-precipitates with Csp24 and co-localizes with it in the cytosol of type-B photoreceptor cell bodies. Several signal transduction pathways have been shown to regulate the phosphorylation of Csp24 and contribute to cellular plasticity. Here, we report the identification of the adapter protein 14-3-3 in lysates of the Hermissenda circumesophageal nervous system and its interaction with Csp24. Immunoprecipitation experiments using an antibody that is broadly reactive with several isoforms of the 14-3-3 family of proteins showed that Csp24 co-precipitates with 14-3-3 protein, and nervous systems stimulated with 5-HT exhibited a significant increase in co-precipitated Csp24 probed with a phosphospecific antibody as compared with controls. These results indicate that post-translational modifications of Csp24 regulate its interaction with 14-3-3 protein, and suggest that this mechanism may contribute to the control of intrinsic enhanced excitability.

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One‐Trial In Vitro Conditioning of Hermissenda Regulates Phosphorylation of Ser‐122 of Csp24

Cited by 5 publications

References 36 publications

Proteomic analysis of short- and intermediate-term memory in Hermissenda

Proteomic analysis of short- and intermediate-term memory in Hermissenda

Proteomic analysis of post-translational modifications in conditioned Hermissenda

14-3-3 proteins interact with the β-thymosin repeat protein Csp24

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