TY - JOUR
T1 - Amelin and synapsin I are 4.1 related spectrin binding proteins in brain
AU - Krebs, Keith E.
AU - Zagon, Ian S.
AU - Goodman, Steven R.
N1 - Funding Information:
This work was supportedi n part by a fellowship from the AHA South Central PA chapter to K. E. Krebs, National Institutes of Health GrantNs S-19357a nd HL-26059t o S. R. Goodmana nd NS-21246t o I. S. Zagon and S. R. Goodman. S. R. Goodman is an Established Investigatoro f the American Heart Association. We Also thank Patricia McLaughlin and Sue Ditty for technicala ssist-ance, David Sitler for photographica ssistance,a ndJennifer Dimeler for manuscriptp reparation.
PY - 1987/6
Y1 - 1987/6
N2 - How do synaptic vesicles move towards the presynaptic plasma membrane, fuse with that membrane, and release their contents during synaptic transmission? The answers to these questions at the molecular level are just beginning to be understood. Synapsin I is a neuron specific phosphoprotein that is associated with the cytoplasmic surface of synaptic vesicles. During synaptic transmission, the translocation of the synaptic vesicles to the presynaptic membrane of the neuron is thought to be mediated through changes in the phosphorylation state of synapsin I. It has been suggested that synapsin I is a spectrin binding protein related to the erythrocyte cytoskeletal protein 4.1, which binds to the terminal ends of the erythrocyte spectrin tetramer. The interaction of synapsin I (through brain spectrin) with the neuronal cytoskeleton may be essential for regulating the movement of synaptic vesicles towards the presynaptic plasma membrane. In addition, we have identified another protein in brain that is immunologically and structurally more closely related to erythrocyte 4.1 than is synapsin I. This protein, termed amelin, is localized in the cell body and dendrites of the neuron, whereas synapsin I is found exclusively in the synaptic terminals, suggesting that there is a family of erythrocyte 4.1 related proteins present in brain with distinct subcellular distribution and functions.
AB - How do synaptic vesicles move towards the presynaptic plasma membrane, fuse with that membrane, and release their contents during synaptic transmission? The answers to these questions at the molecular level are just beginning to be understood. Synapsin I is a neuron specific phosphoprotein that is associated with the cytoplasmic surface of synaptic vesicles. During synaptic transmission, the translocation of the synaptic vesicles to the presynaptic membrane of the neuron is thought to be mediated through changes in the phosphorylation state of synapsin I. It has been suggested that synapsin I is a spectrin binding protein related to the erythrocyte cytoskeletal protein 4.1, which binds to the terminal ends of the erythrocyte spectrin tetramer. The interaction of synapsin I (through brain spectrin) with the neuronal cytoskeleton may be essential for regulating the movement of synaptic vesicles towards the presynaptic plasma membrane. In addition, we have identified another protein in brain that is immunologically and structurally more closely related to erythrocyte 4.1 than is synapsin I. This protein, termed amelin, is localized in the cell body and dendrites of the neuron, whereas synapsin I is found exclusively in the synaptic terminals, suggesting that there is a family of erythrocyte 4.1 related proteins present in brain with distinct subcellular distribution and functions.
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U2 - 10.1016/0361-9230(87)90218-8
DO - 10.1016/0361-9230(87)90218-8
M3 - Article
C2 - 3113675
AN - SCOPUS:0023228645
SN - 0361-9230
VL - 18
SP - 793
EP - 798
JO - Journal of Electrophysiological Techniques
JF - Journal of Electrophysiological Techniques
IS - 6
ER -