Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations

doi:10.1083/jcb.96.2.443

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Identification of fodrin as a major calmodulin-binding protein in postsynaptic density preparations

RK Carlin, DC Bartelt and P Siekevitz

A major protein of postsynaptic densities (PSDs), a doublet of 230,000 and 235,000 Mr that becomes enriched in PSDs after treatment of synaptic membranes with 0.5% Triton X-100, has been found to be identical to fodrin (Levine, J., and M. Willard, 1981, J. Cell Biol. 90:631) by the following criteria. The upper bands of the PSD doublet and purified fodrin (alpha-fodrin) were found to be identical since both bands (a) co-migrated on SDS gels, (b) reacted with antifodrin, (c) bound calmodulin, and (d) had identical peptide maps after Staphylococcus aureus protease digestion. The lower bands of the PSD doublet and of purified fodrin (beta-fodrin) were found to be identical since both bands co-migrated on SDS gels and both had identical peptide maps after S. aureus protease digestion. The binding of calmodulin to alpha-fodrin was confirmed by cross-linking azido-125I-calmodulin to fodrin before running the protein on SDS gels. No binding of calmodulin to beta-fodrin was observed with either the gel overlay or azido- calmodulin techniques. A second calmodulin binding protein in the PSD has been found to be the proteolytic product of alpha-fodrin. This band (140,000 Mr), which can be created by treating fodrin with chymotrypsin, both binds calmodulin and reacts with antifodrin.
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Hayes, N., Scott, C, Heerkens, E, Ohanian, V, Maggs, A., Pinder, J., Kordeli, E, Baines, A. (2000). Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities. J. Cell Sci. 113: 2023-2034 [Abstract]
Boeckers, T. M., Kreutz, M. R., Winter, C., Zuschratter, W., Smalla, K.-H., Sanmarti-Vila, L., Wex, H., Langnaese, K., Bockmann, J., Garner, C. C., Gundelfinger, E. D. (1999). Proline-Rich Synapse-Associated Protein-1/Cortactin Binding Protein 1 (ProSAP1/CortBP1) Is a PDZ-Domain Protein Highly Enriched in the Postsynaptic Density. J. Neurosci. 19: 6506-6518 [Abstract] [Full Text]
Seidenbecher, C. I., Langnaese, K., Sanmarti-Vila, L., Boeckers, T. M., Smalla, K.-H., Sabel, B. A., Garner, C. C., Gundelfinger, E. D., Kreutz, M. R. (1998). Caldendrin, a Novel Neuronal Calcium-binding Protein Confined to the Somato-dendritic Compartment. J. Biol. Chem. 273: 21324-21331 [Abstract] [Full Text]
Allison, D. W., Gelfand, V. I., Spector, I., Craig, A. M. (1998). Role of Actin in Anchoring Postsynaptic Receptors in Cultured Hippocampal Neurons: Differential Attachment of NMDA versus AMPA Receptors. J. Neurosci. 18: 2423-2436 [Abstract] [Full Text]
Masse, T., Kelly, P. T. (1997). Overexpression of Ca2+/Calmodulin-Dependent Protein Kinase II in PC12 Cells Alters Cell Growth, Morphology, and Nerve Growth Factor-Induced Differentiation. J. Neurosci. 17: 924-931 [Abstract] [Full Text]
Hayashi, K., Ishikawa, R., Ye, L.-H., He, X.-L., Takata, K., Kohama, K., Shirao, T. (1996). Modulatory Role of Drebrin on the Cytoskeleton within Dendritic Spines in the Rat Cerebral Cortex. J. Neurosci. 16: 7161-7170 [Abstract] [Full Text]
Vanderklish, P, Bednarski, E, Lynch, G (1996). Translational suppression of calpain blocks long-term potentiation.. Learn. Mem. 3: 209-217 [Abstract]
Malchiodi-Albedi, F, Ceccarini, M, Winkelmann, J., Morrow, J., Petrucci, T. (1993). The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons. J. Cell Sci. 106: 67-78 [Abstract]
Reichardt, L. (1984). Immunological approaches to the nervous system. Science 225: 1294-1299 [Abstract]
Lynch, G, Baudry, M (1984). The biochemistry of memory: a new and specific hypothesis. Science 224: 1057-1063 [Abstract]
Baitinger, C., Cheney, R., Clements, D., Glicksman, M., Hirokawa, N., Levine, J., Meiri, K., Simon, C., Skene, P., Willard, M. (1983). Axonally Transported Proteins in Axon Development, Maintenance, and Regeneration. Cold Spring Harb Symp Quant Biol 48: 791-802 [Abstract]