title: Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation.
abstract: Synaptogenesis and synaptic plasticity depend crucially on the dynamic and locally specific regulation of the actin cytoskeleton. We identified an important component for controlled actin assembly, abelson interacting protein-1 (Abi-1), as a binding partner for the postsynaptic density (PSD) protein ProSAP2/Shank3. During early neuronal development, Abi-1 is localized in neurites and growth cones; at later stages, the protein is enriched in dendritic spines and PSDs, as are components of a trimeric complex consisting of Abi-1, Eps8 and Sos-1. Abi-1 translocates upon NMDA application from PSDs to nuclei. Nuclear entry depends on abelson kinase activity. Abi-1 co-immunoprecipitates with the transcription factor complex of Myc/Max proteins and enhances E-box-regulated gene transcription. Downregulation of Abi-1 by small interfering RNA results in excessive dendrite branching, immature spine and synapse morphology and a reduction of synapses, whereas overexpression of Abi-1 has the opposite effect. Data show that Abi-1 can act as a specific synapto-nuclear messenger and is essentially involved in dendrite and synapse formation.
authors.affiliation: Institute for Anatomy and Cell Biology, Ulm University, Ulm, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Proepper
authors.forename: Svenja
authors.initials: S
authors.lastname: Johannsen
authors.forename: Stefan
authors.initials: S
authors.lastname: Liebau
authors.forename: Janine
authors.initials: J
authors.lastname: Dahl
authors.forename: Bianca
authors.initials: B
authors.lastname: Vaida
authors.forename: Juergen
authors.initials: J
authors.lastname: Bockmann
authors.forename: Michael R
authors.initials: MR
authors.lastname: Kreutz
authors.forename: Eckart D
authors.initials: ED
authors.lastname: Gundelfinger
authors.forename: Tobias M
authors.initials: TM
authors.lastname: Boeckers
mesh_terms: D000199:Actins / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D001921:Brain / Q000187:drug effects / Q000378:metabolism; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D003712:Dendrites / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D016202:N-Methylaspartate / Q000494:pharmacology; D009419:Nerve Tissue Proteins / Q000235:genetics / Q000378:metabolism; D009474:Neurons / Q000187:drug effects / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011392:Proline / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013569:Synapses / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D020798:Two-Hybrid System Techniques; D014443:Tyrosine / Q000737:chemistry / Q000378:metabolism
chemical_list: D000199:Actins; D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; C120532:Shank3 protein, rat; C033652:postsynaptic density proteins; D049452:Green Fluorescent Proteins; D014443:Tyrosine; D016202:N-Methylaspartate; D011392:Proline