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  1. AU="Ananda, Virly Y"
  2. AU="Wenwu Xie"
  3. AU=Greenwood Jonathan
  4. AU="Mella, Sebastian"
  5. AU="Pogurschi, Elena"
  6. AU="Ali, Athar"
  7. AU="Chen, DeChao"
  8. AU=Markman Maurie
  9. AU="Tembo, Yamanya"
  10. AU="Vogel, Gretchen"
  11. AU="Bernd W Böttiger"
  12. AU="Burk, Robert D"
  13. AU=Hussain Mushtaq AU=Hussain Mushtaq
  14. AU="Reuter, Susanne"
  15. AU="Thomas P. Quinn"
  16. AU="Grant, April"
  17. AU="Naddaf, Elie"
  18. AU="Park, Do-Hyun"
  19. AU="Posti, Jussi P"
  20. AU="Singh, Gargi"
  21. AU="Fuhrman, Dana Y"
  22. AU="Cholak, Spencer"
  23. AU="Tanowitz, Herbert B."
  24. AU="Gao, Jia-Pei"
  25. AU="Alvarez-Lerma, Francisco"
  26. AU="Junno, Juho-Antti"
  27. AU="Livermore, Polly"
  28. AU="Pervin, Irin"
  29. AU=Upadhyay Avnish K AU=Upadhyay Avnish K
  30. AU="Yabu, Hiroshi"
  31. AU="Soares, Mario J."
  32. AU="Haeusler, Gabrielle M"
  33. AU="Wang, Weiqing"
  34. AU="Fehr, Fabio"
  35. AU="Sasirekha, R" AU="Sasirekha, R"
  36. AU="Rajendraprasad, Girish"
  37. AU="Golbek, Thaddeus W"
  38. AU="Pranav Keshan"

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  1. Artikel: Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation.

    Bell, Tristan A / Luce, Bridget E / Hakim, Pusparanee / Ananda, Virly Y / Dardari, Hiba / Nguyen, Tran H / Monshizadeh, Arezu / Chao, Luke H

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Prominin-1 (Prom1) is a five-transmembrane-pass integral membrane protein that associates with curved regions of the plasma membrane. Prom1 interacts with membrane cholesterol and actively remodels the plasma membrane. Membrane bending activity is ... ...

    Abstract Prominin-1 (Prom1) is a five-transmembrane-pass integral membrane protein that associates with curved regions of the plasma membrane. Prom1 interacts with membrane cholesterol and actively remodels the plasma membrane. Membrane bending activity is particularly evident in photoreceptors, where Prom1 loss-of-function mutations cause failure of outer segment homeostasis, leading to cone-rod retinal dystrophy (CRRD). The Tweety Homology (Ttyh) protein family has been proposed to be homologous to Prominin, but it is not known whether Ttyh proteins have an analogous membrane-bending function. Here, we characterize the membrane-bending activity of human Prom1 and Ttyh1 in native bilayer membranes. We find that Prom1 and Ttyh1 both induce formation of extracellular vesicles (EVs) in cultured mammalian cells and that the EVs produced are biophysically similar. Ttyh1 is more abundant in EV membranes than Prom1 and produces EVs with membranes that are more tubulated than Prom1 EVs. We further show that Prom1 interacts more stably with membrane cholesterol than Ttyh1 and that this may contribute to membrane bending inhibition in Prom1 EVs. Intriguingly, a loss-of-function mutation in Prom1 associated with CRRD induces particularly stable cholesterol binding. These experiments provide mechanistic insight into Prominin function in CRRD and suggest that Prom and Ttyh belong to a single family of functionally related membrane-bending, EV-generating proteins.
    Sprache Englisch
    Erscheinungsdatum 2024-02-28
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.11.08.566258
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Cell wall synthesis and remodelling dynamics determine division site architecture and cell shape in Escherichia coli.

    Navarro, Paula P / Vettiger, Andrea / Ananda, Virly Y / Llopis, Paula Montero / Allolio, Christoph / Bernhardt, Thomas G / Chao, Luke H

    Nature microbiology

    2022  Band 7, Heft 10, Seite(n) 1621–1634

    Abstract: The bacterial division apparatus catalyses the synthesis and remodelling of septal peptidoglycan (sPG) to build the cell wall layer that fortifies the daughter cell poles. Understanding of this essential process has been limited by the lack of native ... ...

    Abstract The bacterial division apparatus catalyses the synthesis and remodelling of septal peptidoglycan (sPG) to build the cell wall layer that fortifies the daughter cell poles. Understanding of this essential process has been limited by the lack of native three-dimensional views of developing septa. Here, we apply state-of-the-art cryogenic electron tomography (cryo-ET) and fluorescence microscopy to visualize the division site architecture and sPG biogenesis dynamics of the Gram-negative bacterium Escherichia coli. We identify a wedge-like sPG structure that fortifies the ingrowing septum. Experiments with strains defective in sPG biogenesis revealed that the septal architecture and mode of division can be modified to more closely resemble that of other Gram-negative (Caulobacter crescentus) or Gram-positive (Staphylococcus aureus) bacteria, suggesting that a conserved mechanism underlies the formation of different septal morphologies. Finally, analysis of mutants impaired in amidase activation (ΔenvC ΔnlpD) showed that cell wall remodelling affects the placement and stability of the cytokinetic ring. Taken together, our results support a model in which competition between the cell elongation and division machineries determines the shape of cell constrictions and the poles they form. They also highlight how the activity of the division system can be modulated to help generate the diverse array of shapes observed in the bacterial domain.
    Mesh-Begriff(e) Amidohydrolases ; Cell Division ; Cell Shape ; Cell Wall ; Escherichia coli/physiology ; Peptidoglycan
    Chemische Substanzen Peptidoglycan ; Amidohydrolases (EC 3.5.-)
    Sprache Englisch
    Erscheinungsdatum 2022-09-12
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ISSN 2058-5276
    ISSN (online) 2058-5276
    DOI 10.1038/s41564-022-01210-z
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: In situ architecture of Opa1-dependent mitochondrial cristae remodeling.

    Fry, Michelle Y / Navarro, Paula P / Hakim, Pusparanee / Ananda, Virly Y / Qin, Xingping / Landoni, Juan C / Rath, Sneha / Inde, Zintis / Lugo, Camila Makhlouta / Luce, Bridget E / Ge, Yifan / McDonald, Julie L / Ali, Ilzat / Ha, Leillani L / Kleinstiver, Benjamin P / Chan, David C / Sarosiek, Kristopher A / Chao, Luke H

    The EMBO journal

    2024  Band 43, Heft 3, Seite(n) 391–413

    Abstract: Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms in the mitochondrion, a membrane-anchored long form (l- ... ...

    Abstract Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms in the mitochondrion, a membrane-anchored long form (l-Opa1) and a processed short form (s-Opa1). The mechanisms for how Opa1 influences cristae shape have remained unclear due to lack of native three-dimensional views of cristae. We perform in situ cryo-electron tomography of cryo-focused ion beam milled mouse embryonic fibroblasts with defined Opa1 states to understand how each form of Opa1 influences cristae architecture. In our tomograms, we observe a variety of cristae shapes with distinct trends dependent on s-Opa1:l-Opa1 balance. Increased l-Opa1 levels promote cristae stacking and elongated mitochondria, while increased s-Opa1 levels correlated with irregular cristae packing and round mitochondria shape. Functional assays indicate a role for l-Opa1 in wild-type apoptotic and calcium handling responses, and show a compromised respiratory function under Opa1 imbalance. In summary, we provide three-dimensional visualization of cristae architecture to reveal relationships between mitochondrial ultrastructure and cellular function dependent on Opa1-mediated membrane remodeling.
    Mesh-Begriff(e) Animals ; Mice ; Fibroblasts/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism
    Chemische Substanzen Mitochondrial Proteins
    Sprache Englisch
    Erscheinungsdatum 2024-01-15
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/s44318-024-00027-2
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: In situ

    Fry, Michelle Y / Navarro, Paula P / Hakim, Pusparanee / Ananda, Virly Y / Qin, Xingping / Landoni, Juan C / Rath, Sneha / Inde, Zintis / Lugo, Camila Makhlouta / Luce, Bridget E / Ge, Yifan / McDonald, Julie L / Ali, Ilzat / Ha, Leillani L / Kleinstiver, Benjamin P / Chan, David C / Sarosiek, Kristopher A / Chao, Luke H

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms in the mitochondrion, a membrane-anchored long form (l- ... ...

    Abstract Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms in the mitochondrion, a membrane-anchored long form (l-Opa1) and a processed short form (s-Opa1). The mechanisms for how Opa1 influences cristae shape have remained unclear due to lack of native three-dimensional views of cristae. We perform
    Sprache Englisch
    Erscheinungsdatum 2023-11-09
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2023.01.16.524176
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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