[HTML][HTML] Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin
T Coppola, S Magnin-Luthi, V Perret-Menoud… - Journal of Biological …, 2001 - ASBMB
To define the role of the Rab3-interacting molecule RIM in exocytosis we searched for
additional binding partners of the protein. We found that the two C 2 domains of RIM display
properties analogous to those of the C 2 B domain of synaptotagmin-I. Thus, RIM-C 2 A and
RIM-C 2 B bind in a Ca 2+-independent manner to α1B, the pore-forming subunit of N-type
Ca 2+ channels (EC 50=∼ 20 nm). They also weakly interact with the α1C but not the α1D
subunit of L-type Ca 2+ channels. In addition, the C 2 domains of RIM associate with SNAP …
additional binding partners of the protein. We found that the two C 2 domains of RIM display
properties analogous to those of the C 2 B domain of synaptotagmin-I. Thus, RIM-C 2 A and
RIM-C 2 B bind in a Ca 2+-independent manner to α1B, the pore-forming subunit of N-type
Ca 2+ channels (EC 50=∼ 20 nm). They also weakly interact with the α1C but not the α1D
subunit of L-type Ca 2+ channels. In addition, the C 2 domains of RIM associate with SNAP …