Rim and exocytosis: Rab3a-binding and secretion-enhancing domains are separate and function independently.
Rim1 has been identified in brain by its ability to bind Rab3a-GTP and has been postulated to be a Rab3a effector protein. Like Rabphilin3, another putative Rab3a effector protein, Rim1 modulates secretion and contains a zinc-finger and two C2 domains. We have investigated the structural basis for the ability of Rim1 to bind Rab3a-GTP and to stimulate exocytosis in chromaffin cells.
Sun
Lei
L
Department of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0632, USA.
Bittner
Mary A
MA
Holz
Ronald W
RW
D020816:Amino Acid Motifs; D000818:Animals; D002118:Calcium / Q000378:metabolism; D019439:Chromaffin Cells; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D005089:Exocytosis; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D017353:Gene Deletion; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016335:Zinc Fingers; D020826:rab3A GTP-Binding Protein / Q000378:metabolism*
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D006160:Guanosine Triphosphate; D020826:rab3A GTP-Binding Protein; D002118:Calcium