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Phosphatase and tensin homologue (PTEN) regulates synaptic plasticity independently of its effect on neuronal morphology and migration
Author(s) -
Sperow Margaret,
Berry Raymond B.,
Bayazitov Ildar T.,
Zhu Guo,
Baker Suzanne J.,
Zakharenko Stanislav S.
Publication year - 2012
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.220236
Subject(s) - tensin , pten , synaptic plasticity , neuroscience , biology , synaptic augmentation , phosphatase , synaptic fatigue , neuroplasticity , nonsynaptic plasticity , microbiology and biotechnology , metaplasticity , signal transduction , excitatory postsynaptic potential , pi3k/akt/mtor pathway , phosphorylation , inhibitory postsynaptic potential , receptor , genetics
Non‐technical summary The sizes of neurons and their synaptic connections are regulated by multiple molecular mechanisms to provide neuronal networks that perform well‐defined functions. Deletion of the tumour suppressor phosphatase and tensin homologue (PTEN) during early development leads to a 2‐ to 3‐fold increase in neuronal and synaptic size and abnormalities in synaptic plasticity, the cellular mechanism underlying learning and memory. Whether PTEN deletion affects synaptic plasticity directly or as a consequence of its effect on the neuronal and synaptic size remained unclear. Here we show that deletion of the Pten gene Pten in mice during postnatal development, when the central nervous system is formed, does not affect neuronal or synaptic size but impairs synaptic plasticity. Thus, PTEN affects neuronal structure and synaptic plasticity through independent mechanisms.