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Hippocampal protein‐protein interactions in spatial memory
Author(s) -
Nelson Thomas J.,
Backlund Peter S.,
Alkon Daniel L.
Publication year - 2004
Publication title -
hippocampus
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.767
H-Index - 155
eISSN - 1098-1063
pISSN - 1050-9631
DOI - 10.1002/hipo.10152
Subject(s) - neuroscience , memory consolidation , protein–protein interaction , biology , hippocampal formation , stathmin , chemistry , microbiology and biotechnology , microtubule , hippocampus
Memory consolidation in mammalian brain is accompanied by widespread reorganization of synaptic contacts and dendritic structure. Understanding of the protein‐protein interactions that underlie these structural changes has been hampered by the difficulty of studying protein‐protein interactions produced in vivo by signaling, learning, and other physiological responses using current methodologies. Using a novel technique that separates interacting proteins from noninteracting proteins on the basis of their protein‐target affinity, we identified 16 proteins for which protein‐target binding is altered in vivo by spatial learning, including stathmin, complexin I, 14‐3‐3, and several structural proteins including F‐actin capping protein, tubulin, GFAP, and actin. Interactions between complexin and its targets (p25α and Drac1‐like protein) and the interaction between CapZ and tubulin were calcium‐dependent. The preponderance of structural proteins and proteins involved in synapse formation and reorganization of growth cones among proteins undergoing memory‐specific changes in protein‐protein interactions suggests that synaptic structural reorganization is a predominant feature of the consolidation phase of memory. © 2004 Wiley‐Liss, Inc.