Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Nadav Shai; Eden Yifrach; Carlo W. T. van Roermund; Nir Cohen; Chen Bibi; Lodewijk Ijlst; Laetitia Cavellini; Julie Meurisse; Ramona Schuster; Lior Zada; Muriel C. Mari; Fulvio M. Reggiori; Adam L. Hughes; Mafalda Escobar-Henriques; Mickael M. Cohen; Hans R. Waterham; Ronald J. A. Wanders; Maya Schuldiner; Einat Zalckvar

doi:10.1038/s41467-018-03957-8

Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Nadav Shai, Eden Yifrach, Carlo W. T. van Roermund, Nir Cohen, Chen Bibi, Lodewijk Ijlst, Laetitia Cavellini, Julie Meurisse, Ramona Schuster, Lior Zada, Muriel C. Mari, Fulvio M. Reggiori, Adam L. Hughes, Mafalda Escobar-Henriques, Mickael M. Cohen, Hans R. Waterham, Ronald J. A. Wanders, Maya Schuldiner, Einat Zalckvar

Weizmann Institute of Science

Research output: Contribution to journal › Article › peer-review

Abstract

The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in beta-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease.

Original language	English
Article number	1761
Number of pages	13
Journal	Nature Communications
Volume	9
Issue number	1
DOIs	https://doi.org/10.1038/s41467-018-03957-8
State	Published - 2 May 2018

All Science Journal Classification (ASJC) codes

General Chemistry
General Biochemistry,Genetics and Molecular Biology
General Physics and Astronomy

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Shai, N., Yifrach, E., van Roermund, C. W. T., Cohen, N., Bibi, C., Ijlst, L., Cavellini, L., Meurisse, J., Schuster, R., Zada, L., Mari, M. C., Reggiori, F. M., Hughes, A. L., Escobar-Henriques, M., Cohen, M. M., Waterham, H. R., Wanders, R. J. A., Schuldiner, M., & Zalckvar, E. (2018). Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact. Nature Communications, 9(1), Article 1761. https://doi.org/10.1038/s41467-018-03957-8

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title = "Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact",

abstract = "The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in beta-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease.",

author = "Nadav Shai and Eden Yifrach and {van Roermund}, {Carlo W. T.} and Nir Cohen and Chen Bibi and Lodewijk Ijlst and Laetitia Cavellini and Julie Meurisse and Ramona Schuster and Lior Zada and Mari, {Muriel C.} and Reggiori, {Fulvio M.} and Hughes, {Adam L.} and Mafalda Escobar-Henriques and Cohen, {Mickael M.} and Waterham, {Hans R.} and Wanders, {Ronald J. A.} and Maya Schuldiner and Einat Zalckvar",

note = "Publisher Copyright: {\textcopyright} 2018 The Author(s).",

year = "2018",

month = may,

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doi = "10.1038/s41467-018-03957-8",

language = "الإنجليزيّة",

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Shai, N, Yifrach, E, van Roermund, CWT, Cohen, N, Bibi, C, Ijlst, L, Cavellini, L, Meurisse, J, Schuster, R, Zada, L, Mari, MC, Reggiori, FM, Hughes, AL, Escobar-Henriques, M, Cohen, MM, Waterham, HR, Wanders, RJA, Schuldiner, M & Zalckvar, E 2018, 'Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact', Nature Communications, vol. 9, no. 1, 1761. https://doi.org/10.1038/s41467-018-03957-8

TY - JOUR

T1 - Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

AU - Shai, Nadav

AU - Yifrach, Eden

AU - van Roermund, Carlo W. T.

AU - Cohen, Nir

AU - Bibi, Chen

AU - Ijlst, Lodewijk

AU - Cavellini, Laetitia

AU - Meurisse, Julie

AU - Schuster, Ramona

AU - Zada, Lior

AU - Mari, Muriel C.

AU - Reggiori, Fulvio M.

AU - Hughes, Adam L.

AU - Escobar-Henriques, Mafalda

AU - Cohen, Mickael M.

AU - Waterham, Hans R.

AU - Wanders, Ronald J. A.

AU - Schuldiner, Maya

AU - Zalckvar, Einat

PY - 2018/5/2

Y1 - 2018/5/2

N2 - The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in beta-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease.

AB - The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in beta-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease.

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DO - 10.1038/s41467-018-03957-8

M3 - مقالة

SN - 2041-1723

VL - 9

JO - Nature Communications

JF - Nature Communications

IS - 1

M1 - 1761

ER -

Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Abstract

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