The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis

• Published in: The Journal of biological chemistry Vol. 274; no. 37; pp. 25963 - 25966
• Main Authors: Lai, Michael M., Hong, Jenny J., Ruggiero, Alicia M., Burnett, Patrick E., Slepnev, Vladimir I., De Camilli, Pietro, Snyder, Solomon H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.09.1999; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Calcineurin - metabolism; Calcium - metabolism; Clathrin - antagonists & inhibitors; Clathrin - metabolism; Dynamin I; Dynamins; Endocytosis; Glutathione Transferase - metabolism; GTP Phosphohydrolases - metabolism; Humans; Immunophilins - metabolism; Rats; Recombinant Fusion Proteins - metabolism; Synaptic Vesicles - metabolism; Tacrolimus Binding Proteins
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.37.25963

Exocytosis of synaptic vesicles is calcium-dependent, with synaptotagmin serving as the calcium sensor. Endocytosis of synaptic vesicles has also been postulated as a calcium-dependent process; however, an endocytic calcium sensor has not been found. We now report a physical association between the calcium-dependent phosphatase calcineurin and dynamin 1, a component of the synaptic endocytic machinery. The calcineurin-dynamin 1 interaction is calcium-dependent, with an EC50 for calcium in the range of 0.1–0.4 μm. Disruption of the calcineurin-dynamin 1 interaction inhibits clathrin-mediated endocytosis. Thus, the calcium-dependent formation of the calcineurin-dynamin 1 complex, delivered to the other endocytic coat proteins, provides a calcium-sensing mechanism that facilitates endocytosis.