Dephosphorylation and internalization of cell adhesion molecule L1 induced by theta burst stimulation in rat hippocampus.
The neural cell adhesion molecule L1 may participate in initiating and maintaining synaptic changes during learning in the hippocampus. One prominent form of synaptic change in the hippocampus is long-term potentiation (LTP) that occurs following specific patterns of synaptic activity. We present evidence that Y1176 of the YRSL motif within L1 cytoplasmic domain is dephosphorylated in LTP-induced hippocampus. The dephosphorylated L1 is associated with AP-2 and AP180 that are required for clathrin-mediated internalization of L1. These data suggest that clathrin-mediated recycling of L1 at presynaptic sites is enhanced by certain kinds of neural activity, and that maintenance of LTP-induced synaptic changes is regulated by L1 recycling.
Itoh
Kouichi
K
Laboratory of Molecular Pharmacology, Department of Pharmaceutical Technology, Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University, Kagawa 769-2193, Japan.
Shimono
Ken
K
Lemmon
Vance
V
D033962:Adaptor Protein Complex 2 / Q000378:metabolism; D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D022163:Clathrin-Coated Vesicles / Q000378:metabolism*; D004558:Electric Stimulation; D004705:Endocytosis / Q000502:physiology*; D006624:Hippocampus / Q000378:metabolism* / Q000503:physiopathology; D017774:Long-Term Potentiation / Q000502:physiology*; D034041:Monomeric Clathrin Assembly Proteins / Q000378:metabolism; D039842:Neural Cell Adhesion Molecule L1 / Q000378:metabolism*; D009924:Organ Culture Techniques; D010766:Phosphorylation; D017434:Protein Structure, Tertiary / Q000502:physiology; D051381:Rats; D017207:Rats, Sprague-Dawley; D013569:Synapses / Q000378:metabolism*; D013826:Theta Rhythm
D033962:Adaptor Protein Complex 2; D034041:Monomeric Clathrin Assembly Proteins; D039842:Neural Cell Adhesion Molecule L1; C439023:clathrin assembly protein AP180