The multifunctional nature of mitochondrial contact site proteins

Clare S. Harper; Antoineen J. White; Laura L. Lackner

doi:10.1016/j.ceb.2020.02.010

The multifunctional nature of mitochondrial contact site proteins

Clare S. Harper, Antoineen J. White, Laura L. Lackner^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Review article › peer-review

22 Scopus citations

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.

Original language	English (US)
Pages (from-to)	58-65
Number of pages	8
Journal	Current Opinion in Cell Biology
Volume	65
DOIs	https://doi.org/10.1016/j.ceb.2020.02.010
State	Published - Aug 2020

Funding

We would like to thank members of the Lackner Lab for helpful discussions. We would like to apologize to colleagues whose outstanding work on mitochondria-organelle contacts could not be included due to space limitations. This work has been supported in part by funding from the NIH NIGMS Training Grant T32GM008382 to AJW, the NIH NIGMS Training Grant T32GM008449, and National Science Foundation Graduate Research Fellowship DGE-1842165 to CSH, and the NIH NIGMS grant R01GM120303 to LLL. We would like to thank members of the Lackner Lab for helpful discussions. We would like to apologize to colleagues whose outstanding work on mitochondria-organelle contacts could not be included due to space limitations. This work has been supported in part by funding from the NIH NIGMS Training Grant T32GM008382 to AJW, the NIH NIGMS Training Grant T32GM008449 , and National Science Foundation Graduate Research Fellowship DGE-1842165 to CSH, and the NIH NIGMS grant R01GM120303 to LLL .

Keywords

Membrane contact sites
Mitochondria
Mitochondrial contact sites

ASJC Scopus subject areas

Cell Biology

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10.1016/j.ceb.2020.02.010

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title = "The multifunctional nature of mitochondrial contact site proteins",

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.",

keywords = "Membrane contact sites, Mitochondria, Mitochondrial contact sites",

author = "Harper, {Clare S.} and White, {Antoineen J.} and Lackner, {Laura L.}",

note = "Funding Information: We would like to thank members of the Lackner Lab for helpful discussions. We would like to apologize to colleagues whose outstanding work on mitochondria-organelle contacts could not be included due to space limitations. This work has been supported in part by funding from the NIH NIGMS Training Grant T32GM008382 to AJW, the NIH NIGMS Training Grant T32GM008449, and National Science Foundation Graduate Research Fellowship DGE-1842165 to CSH, and the NIH NIGMS grant R01GM120303 to LLL. Funding Information: We would like to thank members of the Lackner Lab for helpful discussions. We would like to apologize to colleagues whose outstanding work on mitochondria-organelle contacts could not be included due to space limitations. This work has been supported in part by funding from the NIH NIGMS Training Grant T32GM008382 to AJW, the NIH NIGMS Training Grant T32GM008449 , and National Science Foundation Graduate Research Fellowship DGE-1842165 to CSH, and the NIH NIGMS grant R01GM120303 to LLL . Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",

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AU - Lackner, Laura L.

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N2 - 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.

AB - 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.

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The multifunctional nature of mitochondrial contact site proteins

Abstract

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Keywords

ASJC Scopus subject areas

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