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  1. Article ; Online: The Expanding and Unexpected Functions of Mitochondria Contact Sites.

    Lackner, Laura L

    Trends in cell biology

    2019  Volume 29, Issue 7, Page(s) 580–590

    Abstract: Mitochondria make functionally relevant contacts with most, if not all, other organelles in the cell. These contacts impact on mitochondrial behavior and function as well as on a wide variety of cellular functions. Many recent advances have been made in ... ...

    Abstract Mitochondria make functionally relevant contacts with most, if not all, other organelles in the cell. These contacts impact on mitochondrial behavior and function as well as on a wide variety of cellular functions. Many recent advances have been made in the rapidly growing field of mitochondria contact site biology, and these advances have expanded the known functions of mitochondria contact sites in exciting and unexpected ways.
    MeSH term(s) Humans ; Mitochondria/metabolism ; Organelles/metabolism
    Language English
    Publishing date 2019-03-28
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2019.02.009
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Temporal control of contact site formation reveals a relationship between mitochondrial division and Num1-mediated mitochondrial tethering.

    Harper, Clare S / Casler, Jason C / Lackner, Laura L

    Molecular biology of the cell

    2023  Volume 34, Issue 11, Page(s) ar108

    Abstract: Mitochondrial division is critical for maintenance of mitochondrial morphology and cellular homeostasis. Previous studies have suggested that the mitochondria-ER-cortex anchor (MECA), a tripartite membrane contact site between mitochondria, the ER, and ... ...

    Abstract Mitochondrial division is critical for maintenance of mitochondrial morphology and cellular homeostasis. Previous studies have suggested that the mitochondria-ER-cortex anchor (MECA), a tripartite membrane contact site between mitochondria, the ER, and the plasma membrane, is involved in mitochondrial division. However, its role is poorly understood. We developed a system to control MECA formation and depletion, which allowed us to investigate the relationship between MECA-mediated contact sites and mitochondrial division. Num1 is the protein that mediates mitochondria-ER-plasma membrane tethering at MECA sites. Using both rapamycin-inducible dimerization and auxin-inducible degradation components coupled with Num1, we developed systems to temporally control the formation and depletion of the native contact site. Additionally, we designed a regulatable Num1-independant mitochondria-PM tether. We found that mitochondria-PM tethering alone is not sufficient to rescue mitochondrial division and that a specific feature of Num1-mediated tethering is required. This study demonstrates the utility of systems that regulate contact-site formation and depletion in studying the biological functions of membrane contact sites.
    MeSH term(s) Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Cell Membrane/metabolism ; Mitochondrial Proteins/metabolism
    Chemical Substances Saccharomyces cerevisiae Proteins ; Mitochondrial Proteins
    Language English
    Publishing date 2023-08-16
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E23-05-0168
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  3. Article ; Online: Cnm1: A bridge between mitochondria and nuclear ER.

    Casler, Jason C / Lackner, Laura L

    The Journal of cell biology

    2021  Volume 220, Issue 11

    Abstract: Few membrane contact sites have been defined at the molecular level. By using a high-throughput, microscopy-based screen, Eisenberg-Bord, Zung et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202104100) identify Cnm1 as a novel tethering protein ... ...

    Abstract Few membrane contact sites have been defined at the molecular level. By using a high-throughput, microscopy-based screen, Eisenberg-Bord, Zung et al. (2021. J. Cell Biol.https://doi.org/10.1083/jcb.202104100) identify Cnm1 as a novel tethering protein that mediates contact between mitochondria and the nuclear ER in response to phospholipid levels.
    MeSH term(s) Membranes ; Mitochondria ; Mitochondrial Membranes ; Proteins
    Chemical Substances Proteins
    Language English
    Publishing date 2021-10-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202109021
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  4. Article ; Online: Hierarchical integration of mitochondrial and nuclear positioning pathways by the Num1 EF hand.

    Anderson, Heidi L / Casler, Jason C / Lackner, Laura L

    Molecular biology of the cell

    2022  Volume 33, Issue 2, Page(s) ar20

    Abstract: Positioning organelles at the right place and time is critical for their function and inheritance. In budding yeast, mitochondrial and nuclear positioning require the anchoring of mitochondria and dynein to the cell cortex by clusters of Num1. We have ... ...

    Abstract Positioning organelles at the right place and time is critical for their function and inheritance. In budding yeast, mitochondrial and nuclear positioning require the anchoring of mitochondria and dynein to the cell cortex by clusters of Num1. We have previously shown that mitochondria drive the assembly of cortical Num1 clusters, which then serve as anchoring sites for mitochondria and dynein. When mitochondrial inheritance is inhibited, mitochondrial-driven assembly of Num1 in buds is disrupted and defects in dynein-mediated spindle positioning are observed. Using a structure-function approach to dissect the mechanism of mitochondria-dependent dynein anchoring, we found that the EF hand-like motif (EFLM) of Num1 and its ability to bind calcium are required to bias dynein anchoring on mitochondria-associated Num1 clusters. Consistently, when the EFLM is disrupted, we no longer observe defects in dynein activity following inhibition of mitochondrial inheritance. Thus, the Num1 EFLM functions to bias dynein anchoring and activity in nuclear inheritance subsequent to mitochondrial inheritance. We hypothesize that this hierarchical integration of organelle positioning pathways by the Num1 EFLM contributes to the regulated order of organelle inheritance during the cell cycle.
    MeSH term(s) Biological Transport ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Cytoskeletal Proteins/metabolism ; Cytoskeletal Proteins/physiology ; Dyneins/metabolism ; EF Hand Motifs/genetics ; EF Hand Motifs/physiology ; Microtubules/metabolism ; Mitochondria/metabolism ; Organelles/physiology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Spindle Apparatus/metabolism
    Chemical Substances Cytoskeletal Proteins ; NUM1 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2022-01-05
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E21-12-0610-T
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  5. Article ; Online: Comprehensive mutation profiling from wastewater in southern Germany extends evidence of circulating SARS-CoV-2 diversity beyond mutations characteristic for Omicron.

    Agrawal, Shelesh / Orschler, Laura / Zachmann, Kira / Lackner, Susanne

    FEMS microbes

    2023  Volume 4, Page(s) xtad006

    Abstract: Tracking SARS-CoV-2 variants in wastewater is primarily performed by detecting characteristic mutations of the variants. Unlike the Delta variant, the emergence of the Omicron variant and its sublineages as variants of concern has posed a challenge in ... ...

    Abstract Tracking SARS-CoV-2 variants in wastewater is primarily performed by detecting characteristic mutations of the variants. Unlike the Delta variant, the emergence of the Omicron variant and its sublineages as variants of concern has posed a challenge in using characteristic mutations for wastewater surveillance. In this study, we monitored the temporal and spatial variation of SARS-CoV-2 variants by including all the detected mutations and compared whether limiting the analyses to characteristic mutations for variants like Omicron impact the outcomes. We collected 24-hour composite samples from 15 wastewater treatment plants (WWTP) in Hesse and sequenced 164 wastewater samples with a targeted sequencing approach from September 2021 to March 2022. Our results show that comparing the number of all the mutations against the number of the characteristic mutations reveals a different outcome. A different temporal variation was observed for the ORF1a and S gene. As Omicron became dominant, we observed an increase in the overall number of mutations. Based on the characteristic mutations of the SARS-CoV-2 variants, a decreasing trend for the number of ORF1a and S gene mutations was noticed, though the number of known characteristic mutations in both genes is higher in Omicron than Delta.
    Language English
    Publishing date 2023-03-03
    Publishing country England
    Document type Journal Article
    ISSN 2633-6685
    ISSN (online) 2633-6685
    DOI 10.1093/femsmc/xtad006
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  6. Article ; Online: A conserved mechanism for mitochondria-dependent dynein anchoring.

    Kraft, Lauren M / Lackner, Laura L

    Molecular biology of the cell

    2019  Volume 30, Issue 5, Page(s) 691–702

    Abstract: Mitochondrial anchors have functions that extend beyond simply positioning mitochondria. In budding yeast, mitochondria drive the assembly of the mitochondrial anchor protein Num1 into clusters, which serve to anchor mitochondria as well as dynein to the ...

    Abstract Mitochondrial anchors have functions that extend beyond simply positioning mitochondria. In budding yeast, mitochondria drive the assembly of the mitochondrial anchor protein Num1 into clusters, which serve to anchor mitochondria as well as dynein to the cell cortex. Here, we explore a conserved role for mitochondria in dynein anchoring by examining the tethering functions of the evolutionarily distant Schizosaccharomyces pombe Num1 homologue. In addition to its function in dynein anchoring, we find that S. pombe Num1, also known as Mcp5, interacts with and tethers mitochondria to the plasma membrane in S. pombe and Saccharomyces cerevisiae. Thus, the mitochondria and plasma membrane-binding domains of the Num1 homologues, as well as the membrane features these domains recognize, are conserved. In S. pombe, we find that mitochondria impact the assembly and cellular distribution of Num1 clusters and that Num1 clusters actively engaged in mitochondrial tethering serve as cortical attachment sites for dynein. Thus, mitochondria play a critical and conserved role in the formation and distribution of dynein-anchoring sites at the cell cortex and, as a consequence, impact dynein function. These findings shed light on an ancient mechanism of mitochondria-dependent dynein anchoring that is conserved over more than 450 million years of evolution, raising the intriguing possibility that the role mitochondria play in dynein anchoring and function extends beyond yeast to higher eukaryotes.
    MeSH term(s) Cell Membrane/metabolism ; Conserved Sequence ; Dyneins/metabolism ; Meiosis ; Membrane Lipids/metabolism ; Mitochondria/metabolism ; Protein Binding ; Protein Domains ; Saccharomyces cerevisiae/metabolism ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/metabolism
    Chemical Substances Membrane Lipids ; Schizosaccharomyces pombe Proteins ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2019-01-16
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E18-07-0466
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  7. Article ; Online: The

    Gibson, Sophia B / Harper, Clare S / Lackner, Laura L / Andersen, Erik C

    microPublication biology

    2021  Volume 2021

    Abstract: To better understand the mechanism of resistance caused by putative interactions between beta-tubulin and benzimidazole compounds, we sought to purify nematode-specific beta-tubulins using heterologous expression after replacement of the ... ...

    Abstract To better understand the mechanism of resistance caused by putative interactions between beta-tubulin and benzimidazole compounds, we sought to purify nematode-specific beta-tubulins using heterologous expression after replacement of the single
    Language English
    Publishing date 2021-06-30
    Publishing country United States
    Document type Journal Article
    ISSN 2578-9430
    ISSN (online) 2578-9430
    DOI 10.17912/micropub.biology.000411
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  8. Article ; Online: Shaping the dynamic mitochondrial network.

    Lackner, Laura L

    BMC biology

    2014  Volume 12, Page(s) 35

    Abstract: In a majority of cell types, mitochondria form highly dynamic, tubular networks. Maintaining the shape of this complex network is critical for both mitochondrial and cellular function and involves the activities of mitochondrial division, fusion, ... ...

    Abstract In a majority of cell types, mitochondria form highly dynamic, tubular networks. Maintaining the shape of this complex network is critical for both mitochondrial and cellular function and involves the activities of mitochondrial division, fusion, motility, and tethering. Recent studies have advanced our understanding of the molecular mechanisms underlying these conserved activities and their integration with cellular needs.
    MeSH term(s) Animals ; Humans ; Mitochondria/metabolism ; Mitochondrial Dynamics ; Models, Biological ; Movement ; Neurons/metabolism ; Saccharomyces cerevisiae/metabolism
    Language English
    Publishing date 2014-05-27
    Publishing country England
    Document type Journal Article ; Review
    ISSN 1741-7007
    ISSN (online) 1741-7007
    DOI 10.1186/1741-7007-12-35
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  9. Article ; Online: The multifunctional nature of mitochondrial contact site proteins.

    Harper, Clare S / White, Antoineen J / Lackner, Laura L

    Current opinion in cell biology

    2020  Volume 65, Page(s) 58–65

    Abstract: Mitochondria make physical contact with nearly every other membrane in the cell, and these contacts have a wide variety of functions that are carried out by proteins that reside at the sites of contact. Over the past decade, tremendous insight into the ... ...

    Abstract Mitochondria make physical contact with nearly every other membrane in the cell, and these contacts have a wide variety of functions that are carried out by proteins that reside at the sites of contact. Over the past decade, tremendous insight into the identity and functions of proteins localized to mitochondrial contact sites has been gained. In doing so, it has become clear that one protein or protein complex can contribute to contact site formation and function in a wide variety of ways. Thus, complex and often surprising relationships between the roles of a mitochondrial contact site and its multifunctional resident proteins continue to be unraveled.
    MeSH term(s) Endoplasmic Reticulum/metabolism ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/metabolism ; Models, Biological
    Chemical Substances Mitochondrial Proteins
    Language English
    Publishing date 2020-03-21
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2020.02.010
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    Zs.A 2963: Show issues Location:
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  10. Article ; Online: The mechanisms and functions of interorganelle interactions.

    Lackner, Laura L / Voeltz, Gia K

    Molecular biology of the cell

    2017  Volume 28, Issue 6, Page(s) 703–704

    MeSH term(s) Animals ; Calcium/metabolism ; Cell Membrane/metabolism ; Congresses as Topic ; Endosomes/metabolism ; Humans ; Organelles/metabolism
    Chemical Substances Calcium (SY7Q814VUP)
    Language English
    Publishing date 2017-03-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E16-11-0799
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