[HTML][HTML] Intra-and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1
PP Zhu, A Patterson, J Stadler, DP Seeburg… - Journal of Biological …, 2004 - ASBMB
Mammalian Drp1 is a dynamin-like GTPase required for mitochondrial fission. Although it
exists primarily as a cytosolic homo-tetramer in vivo, it can also self-assemble into higher
order structures on the mitochondrial outer membrane, where it is required for proper
mitochondrial division. Functional studies and sequence comparisons have revealed four
different structural domains in Drp1, comprising N-terminal GTP-binding, middle, insert B,
and C-terminal GTPase effector (GED) domains. Here we describe an intramolecular …
exists primarily as a cytosolic homo-tetramer in vivo, it can also self-assemble into higher
order structures on the mitochondrial outer membrane, where it is required for proper
mitochondrial division. Functional studies and sequence comparisons have revealed four
different structural domains in Drp1, comprising N-terminal GTP-binding, middle, insert B,
and C-terminal GTPase effector (GED) domains. Here we describe an intramolecular …