Abstract
The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. Post-targeting, Dnm1-dependent division is controlled by the actions of the WD repeat protein, Mdv1, and the mitochondrial tetratricopeptide repeat-like outer membrane protein, Fis1. Our previous studies suggest a model where at this step Mdv1 functions as an adaptor linking Fis1 with Dnm1. To gain insight into the exact role of the Fis1.Mdv1.Dnm1 complex in mitochondrial division, we performed a structure-function analysis of the Mdv1 adaptor. Our analysis suggests that dynamic interactions between Mdv1 and Dnm1 play a key role in division by regulating Dnm1 self-assembly.
Highlights
The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division
Our analysis suggests that dynamic interactions between Mdv1 and Dnm1 play a key role in division by regulating Dnm1 self-assembly
Our analysis suggests that Mdv1 interacts with Dnm1 only when it is self-assembled into GTP-dependent ring-like structures and not when it exists as extended filaments, which form in the absence of GTP
Summary
Genotype ade; leu; his ; trp; ura; can100 MatA W303, except mdv1-⌬ϻhis5ϩ, Mata W303, except mdv1-⌬ϻhis5ϩ, dnm1-⌬ϻhis5ϩ, Mata W303, except dnm1-⌬ϻhis5ϩ, MatA W303, except fis1-⌬ϻhis5ϩ, dnm1-⌬ϻhis5ϩ, Mata PJ69–4A. Mdv WD domain plays both regulatory and structural roles in division via its interaction with Dnm and indicates that membrane division requires a dynamic Mdv1/Dnm interaction. We postulate that the critical activity of Mdv in division is to promote the assembly of Dnm into a division competent spiral-like structure
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
