ArticleMolecular biology of the cell2018
Direct membrane binding and self-interaction contribute to Mmr1 function in mitochondrial inheritance.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Cell membrane asymmetries and cellular aging.The Biochemical journal · 2025Review
- Review
- Article
- Selective retention of dysfunctional mitochondria during asymmetric cell division in yeast.PLoS biology · 2023Article
- Proteolysis of adaptor protein Mmr1 during budding is necessary for mitochondrial homeostasis in Saccharomyces cerevisiae.Nature communications · 2022Article
- Biochemical Characterization of the Num1-Mdm36 Complex at the Mitochondria-Plasma Membrane Contact Site.Molecules and cells · 2021Article
- Dynamic Regulation of Peroxisomes and Mitochondria during Fungal Development.Journal of fungi (Basel, Switzerland) · 2020Review
- Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.The Journal of biological chemistry · 2019Article
- A conserved mechanism for mitochondria-dependent dynein anchoring.Molecular biology of the cell · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial transport and anchoring mechanisms work in concert to position mitochondria to meet cellular needs. In yeast, Mmr1 functions as a mitochondrial adaptor for Myo2 to facilitate actin-based transport of mitochondria to the bud. Posttransport, Mmr1 is proposed to anchor mitochondria at the bud tip. Although both functions require an interaction between Mmr1 and mitochondria, the molecular basis of the Mmr1-mitochondria interaction is poorly understood. Our in vitro phospholipid binding assays indicate Mmr1 can directly interact with phospholipid membranes. Through structure-function studies we identified an unpredicted membrane-binding domain composed of amino acids 76-195 that is both necessary and sufficient for Mmr1 to interact with mitochondria in vivo and liposomes in vitro. In addition, our structure-function analyses indicate that the coiled-coil domain of Mmr1 is necessary and sufficient for Mmr1 self-interaction and facilitates the polarized localization of the protein. Disrupting either the Mmr1-membrane interaction or Mmr1 self-interaction leads to defects in mitochondrial inheritance. Therefore, direct membrane binding and self-interaction are necessary for Mmr1 function in mitochondrial inheritance and are utilized as a means to spatially and temporally regulate mitochondrial positioning.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.