Mitochondria-driven assembly of a cortical anchor for mitochondria and dynein

Kraft, Lauren M.; Lackner, Laura L.

doi:10.1083/jcb.201702022

Cited by 42 publications

(97 citation statements)

References 56 publications

(110 reference statements)

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“…In the vast majority of cells expressing wildtype Num1, the number of mitochondria-associated clusters was equivalent to the total number of clusters per cell (Figure 2(c)), consistent with mitochondria-dependent cluster assembly [17]. In contrast, in all cells expressing PAN, the number of mitochondria-associated clusters was far lower than the total number of clusters per cell (Figure 2(c)).…”

Section: Resultssupporting

confidence: 57%

“…Importantly, we found that mitochondria were also present at the vast majority of sites where cortical dynein foci and PAN clusters colocalized (Figure 4(a and b)). The percent of cortical dynein foci that colocalized with both PAN clusters and mitochondria (~ 84%) was strikingly similar to the percent of cortical dynein foci that colocalized with both wildtype Num1 clusters and mitochondria (~ 86%; Figure 4(a and b)) [17]. This was particularly notable given the fact that only ~ 21% of PAN clusters are mitochondria-associated, while ~ 95% of wildtype Num1 clusters are mitochondria-associated (Figure 2(d)).…”

Section: Resultsmentioning

confidence: 72%

“…In contrast to wildtype Num1, in which the vast majority of clusters are mitochondria-associated, only a subset of PAN clusters are associated with mitochondria (Figure 2(c and d)) [17]. To determine if dynein is indeed anchored by PAN clusters and, if so, whether it exhibits a preference for mitochondria-associated PAN clusters, we simultaneously imaged PAN, Dyn1, and mitochondria.…”

Section: Resultsmentioning

confidence: 99%

“…The PH domain, which binds with high specificity to PI 4,5 P 2 , targets Num1 to the plasma membrane [13,14], where the protein is found in clusters as well as in a pool that is diffusely localized along the plasma membrane and with cortical ER [3,5,10,15,16]. Cluster formation, which is dependent on the CC domain and an interaction with mitochondria (Figure 1(a)), is critical for the function of Num1 in both mitochondria and dynein anchoring [10,11,17]. Cluster formation has been proposed to enhance the interaction between Num1 and its membrane and protein binding partners and, consequently, the ability of Num1 to robustly tether mitochondria and dynein to the cell cortex [10,11].…”

Section: Introductionmentioning

confidence: 99%

“…While dynein is not required for Num1-mediated mitochondrial anchoring [10,11], mitochondria drive the assembly of Num1 clusters that serve as cortical attachment sites for dynein [17]. These results raise the question of whether the role for mitochondria in dynein anchoring is to simply concentrate Num1 or whether mitochondria play an additional role in driving the assembly of a structure competent to tether dynein.…”

Section: Introductionmentioning

confidence: 99%

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The role of mitochondria in anchoring dynein to the cell cortex extends beyond clustering the anchor protein

et al. 2018

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Organelle distribution is regulated over the course of the cell cycle to ensure that each of the cells produced at the completion of division inherits a full complement of organelles. In yeast, the protein Num1 functions in the positioning and inheritance of two essential organelles, mitochondria and the nucleus. Specifically, Num1 anchors mitochondria as well as dynein to the cell cortex, and this anchoring activity is required for proper mitochondrial distribution and dynein-mediated nuclear inheritance. The assembly of Num1 into clusters at the plasma membrane is critical for both of its anchoring functions. We have previously shown that mitochondria drive the assembly of Num1 clusters and that these mitochondria-assembled Num1 clusters serve as cortical attachment sites for dynein. Here we further examine the role for mitochondria in dynein anchoring. Using a GFP-αGFP nanobody targeting system, we synthetically clustered Num1 on eisosomes to bypass the requirement for mitochondria in Num1 cluster formation. Utilizing this system, we found that mitochondria positively impact the ability of synthetically clustered Num1 to anchor dynein and support dynein function even when mitochondria are no longer required for cluster formation. Thus, the role of mitochondria in regulating dynein function extends beyond simply concentrating Num1; mitochondria likely promote an arrangement of Num1 within a cluster that is competent for dynein anchoring. This functional dependency between mitochondrial and nuclear positioning pathways likely serves as a mechanism to order and integrate major cellular organization systems over the course of the cell cycle.

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Section: Resultssupporting

confidence: 57%

Section: Resultsmentioning

confidence: 72%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The role of mitochondria in anchoring dynein to the cell cortex extends beyond clustering the anchor protein

et al. 2018

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Emerging functions of the mitochondria–ER–lipid droplet three‐way junction in coordinating lipid transfer, metabolism, and storage in cells

Monteiro‐Cardoso,

Giordano

2024

FEBS Letters

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Over the past two decades, we have witnessed a growing appreciation for the importance of membrane contact sites (CS) in facilitating direct communication between organelles. CS are tiny regions where the membranes of two organelles meet but do not fuse and allow the transfer of metabolites between organelles, playing crucial roles in the coordination of cellular metabolic activities. The significant advancements in imaging techniques and molecular and cell biology research have revealed that CS are more complex than what originally thought, and as they are extremely dynamic, they can remodel their shape, composition, and functions in accordance with metabolic and environmental changes and can occur between more than two organelles. Here, we describe how recent studies led to the identification of a three‐way mitochondria–ER–lipid droplet CS and discuss the emerging functions of these contacts in maintaining lipid storage, homeostasis, and balance. We also summarize the properties and functions of key protein components localized at the mitochondria–ER–lipid droplet interface, with a special focus on lipid transfer proteins. Understanding tripartite CS is essential for unraveling the complexities of inter‐organelle communication and cooperation within cells.

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Mitochondrial Control of Fungal Cell Walls: Models and Relevance in Fungal Pathogens

Koch

Traven

2019

Current Topics in Microbiology and Immunology

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Mitochondria-driven assembly of a cortical anchor for mitochondria and dynein

Cited by 42 publications

References 56 publications

The role of mitochondria in anchoring dynein to the cell cortex extends beyond clustering the anchor protein

The role of mitochondria in anchoring dynein to the cell cortex extends beyond clustering the anchor protein

Emerging functions of the mitochondria–ER–lipid droplet three‐way junction in coordinating lipid transfer, metabolism, and storage in cells

Mitochondrial Control of Fungal Cell Walls: Models and Relevance in Fungal Pathogens

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