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- Title
Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during synaptogenesis.
- Authors
Costanzo, Roxana V.; Vilá‐Ortíz, Guillermo J.; Perandones, Claudia; Carminatti, Héctor; Matilla, Antoni; Radrizzani, Martín
- Abstract
Anp32e/Cpd1, a member of the acidic nuclear phosphoprotein (Anp)32 family, is characterized by the presence of an amino terminal domain containing four leucine-rich repeats and a carboxyl-terminal low-compositional complexity acidic region. In previous studies performed to understand the biological role of Anp32e/Cpd1, we showed a predominant presence of Anp32e/Cpd1 in the nucleus. However, when Anp32e/Cpd1 is in the cytoplasm, it co-localizes spatially with protein phosphatase 2A (PP2A) near cell membranes, far from the synapses. In the present work, we show that Anp32e/Cpd1 is also present as a membrane-bound 74/76-kDa protein with a widespread distribution in the brain. We reveal that the expression, synthesis and half-life of this high-molecular-weight form of Anp32e/Cpd1 are spatially and temporally correlated with the cerebellar synaptogenesis period. We demonstrate that synaptic Anp32e/Cpd1 co-localizes, interacts and inhibits PP2A activity, and that phosphorylation of Anp32/Cpd1 is required for the Anp32e–PP2A interaction. Also, subcellular localization was shown with electronic microscopy. Finally, we examine Anp32e/Cpd1 and PP2A distribution in two ataxic mutant models, weaver and staggerer, and show that their co-localization in Purkinje cell dendrites depends on parallel fibre/Purkinje cell contacts. Based on these observations, we propose that Anp32e/Cpd1 mediates synaptogenesis process by modulating PP2A activity.
- Subjects
PHOSPHOPROTEIN phosphatases; PHOSPHATASES; SYNAPSES; NERVE endings; NEURAL transmission; NEUROSCIENCES
- Publication
European Journal of Neuroscience, 2006, Vol 23, Issue 2, p309
- ISSN
0953-816X
- Publication type
Article
- DOI
10.1111/j.1460-9568.2005.04555.x