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Ca MKII ‐mediated displacement of AIDA ‐1 out of the postsynaptic density core
Author(s) -
Dosemeci Ayse,
Toy Dana,
Burch Amelia,
Bayer K. Ulrich,
TaoCheng JungHwa
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12334
Subject(s) - postsynaptic density , excitatory postsynaptic potential , postsynaptic potential , chemistry , biophysics , ankyrin repeat , nmda receptor , hippocampal formation , phosphorylation , biochemistry , neuroscience , biology , receptor , gene
Ankyrin repeat and sterile alpha motif domain‐containing protein 1B ( ANKS 1B, also known as AIDA ‐1) is a major component of the postsynaptic density ( PSD ) in excitatory neurons where it concentrates at the electron‐dense core under basal conditions and moves out during activity. This study investigates the molecular mechanism underlying activity‐induced displacement of AIDA ‐1. Experiments with PSD fractions from brain indicate phosphorylation of AIDA ‐1 upon activation of endogenous Ca MKII . Immuno‐electron microscopy studies show that treatment of hippocampal neurons with NMDA results in an ~ 30 nm shift in the median distance of the AIDA ‐1 label from the postsynaptic membrane, an effect that is blocked by the Ca MKII inhibitor tat CN 21. Ca MKII ‐mediated redistribution of AIDA ‐1 is similar to that observed for Syn GAP . Ca MKII ‐mediated removal of two abundant PSD ‐95‐binding proteins from the PSD core during activity is expected to initiate a molecular reorganization at the PSD .