2018
DOI: 10.1016/j.bpj.2017.11.3300
|View full text |Cite
|
Sign up to set email alerts
|

MiD51 and Mff Co-assemble in Cardiolipin-Enriched Membrane Microdomains to Cooperatively Regulate Drp1-Mediated Mitochondrial Fission

Abstract: undergo large shape changes, they exhibit non-trivial surface flows, they undergo phase transitions, and they interact with surrounding objects. Modeling those requires solving coupled partial differential equations on evolving surfaces. This work presents a new, three-dimensional modeling framework to describe and simulate the mechanical behavior of cellular membranes. It is based on advanced, recently developed modeling techniques in mathematics, physics and computational analysis. Its mathematical descripti… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2022
2022
2022
2022

Publication Types

Select...
1

Relationship

0
1

Authors

Journals

citations
Cited by 1 publication
(1 citation statement)
references
References 0 publications
0
1
0
Order By: Relevance
“…The tethering of OMM and IMM is achieved by the function of Opa1 [108]. Once bound to the surface of OMM, Drp1 also interacts with Mff to form a higher-order oligomeric complex [115]. The pool of cardiolipin at the OMM then allows the fully assembled Drp1 to instigate OMM fission [116].…”
Section: Mitochondrial Fissionmentioning
confidence: 99%
“…The tethering of OMM and IMM is achieved by the function of Opa1 [108]. Once bound to the surface of OMM, Drp1 also interacts with Mff to form a higher-order oligomeric complex [115]. The pool of cardiolipin at the OMM then allows the fully assembled Drp1 to instigate OMM fission [116].…”
Section: Mitochondrial Fissionmentioning
confidence: 99%