14-3-3 proteins interact with the beta-thymosin repeat protein Csp24.

Citation data:

Neuroscience letters, ISSN: 0304-3940, Vol: 424, Issue: 1, Page: 6-9

Publication Year:
2007
Usage 65
Abstract Views 65
Captures 2
Readers 2
Citations 3
Citation Indexes 3
Repository URL:
https://digitalcommons.library.tmc.edu/uthmed_docs/96
PMID:
17709188
DOI:
10.1016/j.neulet.2007.07.013
PMCID:
PMC2695760
Author(s):
Crow, Terry; Xue-Bian, Juan-Juan; Neary, Joseph T
Publisher(s):
Elsevier BV; Elsevier Scientific Publishers Ireland
Tags:
Neuroscience; 14-3-3 Proteins; Animals; Ganglia; Invertebrate; Hermissenda; Immunohistochemistry; MAP Kinase Signaling System; Microfilament Proteins; Nervous System; Phosphoproteins; Phosphorylation; Photoreceptor Cells; Protein Processing; Post-Translational; Serotonin; Signal Transduction; Thymosin; Ubiquitins; Medicine and Health Sciences
article description
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.