Identification and Characterization of AplysiaAdducin, an Aplysia Cytoskeletal Protein Homologous to Mammalian Adducins: Increased Phosphorylation at a Protein Kinase C Consensus Site during Long-Term Synaptic Facilitation
- Lore M. Gruenbaum1,
- Diana M. Gilligan2,
- Marina R. Picciotto3,
- Stéphane Marinesco4, and
- Thomas J. Carew4
- 1Boehringer Ingelheim Pharmaceuticals, Ridgefield, Connecticut 06877,
- 2Puget Sound Blood Center, Seattle, Washington 98104,
- 3Department of Psychiatry, Yale University School of Medicine, New Haven, Connecticut 06508, and
- 4Department of Neurobiology and Behavior, Center for Learning and Memory, University of California, Irvine, California 92697-4550
Abstract
Structural changes at synapses are associated with long-term facilitation (LTF) of synaptic transmission between sensory and motor neurons in Aplysia. We have cloned a cDNA encoding Aplysia adducin (ApADD), theAplysia homolog of mammalian adducins that are regulatory components of the membrane cytoskeleton. ApADD is recovered in the particulate fraction of nervous system extracts and is localized predominantly in the submembraneous region of Aplysianeurons. ApADD is phosphorylated in vitro by protein kinase C (PKC) at a site homologous to the in vivo PKC phosphorylation site in mammalian adducins. Phosphorylation of ApADD at this site is also detected in vivo in the intactAplysia nervous system and is increased 18 hr after serotonin-induced LTF. In contrast, there is no change in phosphorylation during short-term facilitation or 1 hr after initial LTF induction. Thus, ApADD is modulated specifically with later phases of LTF and provides an attractive candidate protein that contributes to structural changes accompanying long-lasting synaptic alteration.
- Received September 25, 2002.
- Revision received December 9, 2002.
- Accepted December 18, 2002.
- Copyright © 2003 Society for Neuroscience
