Neuronal protein NP185 in avian and murine cerebellum: expression during development and evidence for its presence in nerve endingsDG Perry, V Hanson, ML Benuck and S Puszkin Department of Pathology, Mount Sinai School of Medicine, New York, NY 10029-6574. The neuronal protein NP185 is a neural tissue-specific protein isolated from clathrin-coated vesicles in brain. Using 8G8, a monoclonal antibody (MAb) characterized in our laboratory, we studied the expression and distribution of neuronal protein NP185 in developing avian cerebellum and in mature murine cerebellum. Furthermore, we compared these parameters to that of synapse-specific neuronal protein, synaptophysin, and an axon-specific (i.e., non-synaptic) neuronal protein, neurofilament NF68. We found that NP185 expression temporally and spatially corresponds to avian cerebellar synaptogenesis. In addition, NP185 distribution parallels synaptophysin distribution throughout development, while differing from that of either unassembled or filamentous forms of NF68. The evidence also suggests that embryonic NP185 expression coincides with synaptogenesis, and that NP185 remains concentrated in the terminal boutons of mature neurons. The synapse specificity of NP185 and the recent biochemical properties reported for this protein support the postulate that this molecule may trigger synaptic events and distinguish structurally and functionally active synapses.
Volume 39,
Issue 11,
pp. 1461-1470,
11/01/1991
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J. R. Morgan, X. Zhao, M. Womack, K. Prasad, G. J. Augustine, and E. M. Lafer A Role for the Clathrin Assembly Domain of AP180 in Synaptic Vesicle Endocytosis J. Neurosci., December 1, 1999; 19(23): 10201 - 10212. [Abstract] [Full Text] [PDF] |
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W. Hao, Z. Luo, L. Zheng, K. Prasad, and E. M. Lafer AP180 and AP-2 Interact Directly in a Complex That Cooperatively Assembles Clathrin J. Biol. Chem., August 6, 1999; 274(32): 22785 - 22794. [Abstract] [Full Text] [PDF] |
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B. Wendland and S. D. Emr Pan1p, Yeast eps15, Functions as a Multivalent Adaptor That Coordinates Protein-Protein Interactions Essential for Endocytosis J. Cell Biol., April 6, 1998; 141(1): 71 - 84. [Abstract] [Full Text] [PDF] |
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W. Hao, Z. Tan, K. Prasad, K. K. Reddy, J. Chen, G. D. Prestwich, J. R. Falck, S. B. Shears, and E. M. Lafer Regulation of AP-3 Function by Inositides. IDENTIFICATION OF PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE AS A POTENT LIGAND J. Biol. Chem., March 7, 1997; 272(10): 6393 - 6398. [Abstract] [Full Text] [PDF] |
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W. Ye and E. M. Lafer Clathrin Binding and Assembly Activities of Expressed Domains of the Synapse-specific Clathrin Assembly Protein AP-3 J. Biol. Chem., May 5, 1995; 270(18): 10933 - 10939. [Abstract] [Full Text] [PDF] |
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W. Ye, N. Ali, M. E. Bembenek, S. B. Shears, and E. M. Lafer Inhibition of Clathrin Assembly by High Affinity Binding of Specific Inositol Polyphosphates to the Synapse-specific Clathrin Assembly Protein AP-3 J. Biol. Chem., January 27, 1995; 270(4): 1564 - 1568. [Abstract] [Full Text] [PDF] |
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