Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 108; no. 31; pp. E392 - E401
• Main Authors: Limbach, Christoph, Laue, Michael M, Wang, Xiaolu, Hu, Bin, Thiede, Nadine, Hultqvist, Greta, Kilimann, Manfred W
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 02.08.2011; National Acad Sciences
• Series: PNAS Plus
• Subjects: Adaptor Proteins, Signal Transducing - metabolism; Animals; Binding Sites; Biological Sciences; Cell Membrane - metabolism; Cell Membrane - ultrastructure; Cytoskeletal Proteins - metabolism; electron microscopy; exocytosis; GTP-Binding Proteins - metabolism; Immunoblotting; Mammals; MEDICIN; MEDICINE; Membranes; Microscopy, Immunoelectron; Molecular structure; Multiprotein Complexes - metabolism; Multiprotein Complexes - ultrastructure; Nerve Tissue Proteins - metabolism; Neuropeptides - metabolism; Neurotransmitter Agents - metabolism; Neurotransmitters; ontogeny; plasma membrane; PNAS Plus; polypeptides; Protein Binding; protein structure; Proteins; Rats; Rats, Sprague-Dawley; scaffolding protein; space and time; Synapses - metabolism; Synapses - ultrastructure; synaptic transmission; topology

The protein machinery of neurotransmitter exocytosis requires efficient orchestration in space and time, for speed and precision of neurotransmission and also for synaptic ontogeny and plasticity. However, its spatial organization in situ is virtually unknown. Aczonin/Piccolo is a putative organizer...