TY - JOUR
T1 - It takes two to tango: The essential role of ER-mitochondrial contact sites in mitochondrial dynamics
AU - Hemel, I.M.G.M.
AU - Sarantidou, R.
AU - Gerards, M.
N1 - Funding Information:
The research presented in this article has been made possible with the support of the Dutch Province of Limburg, the Netherlands .
Publisher Copyright:
© 2021 The Authors
PY - 2021/12/1
Y1 - 2021/12/1
N2 - Mitochondria change their shape, size and number, in response to cellular demand, through mitochondrial dynamics. The interaction between mitochondria and the ER, through ER-mitochondrial contact sites, is crucial in mitochondrial dynamics. Several protein complexes tethering mitochondria to the ER include proteins involved in fission or fusion but also proteins involved in calcium homeostasis, which is known to affect mitochondrial dynamics. The formation of these contact sites are especially important for mitochondrial fission as these contact sites induce both outer and inner membrane constriction, prior to recruitment of Drp1. While the exact molecular mechanisms behind these constrictions remain uncertain, several hypotheses have been proposed. In this review, we discuss the involvement of tethering complexes in mitochondrial dynamics and provide an overview of the current knowledge and hypotheses on the constriction of the outer and inner mitochondrial membrane at ER-mitochondrial contact sites.
AB - Mitochondria change their shape, size and number, in response to cellular demand, through mitochondrial dynamics. The interaction between mitochondria and the ER, through ER-mitochondrial contact sites, is crucial in mitochondrial dynamics. Several protein complexes tethering mitochondria to the ER include proteins involved in fission or fusion but also proteins involved in calcium homeostasis, which is known to affect mitochondrial dynamics. The formation of these contact sites are especially important for mitochondrial fission as these contact sites induce both outer and inner membrane constriction, prior to recruitment of Drp1. While the exact molecular mechanisms behind these constrictions remain uncertain, several hypotheses have been proposed. In this review, we discuss the involvement of tethering complexes in mitochondrial dynamics and provide an overview of the current knowledge and hypotheses on the constriction of the outer and inner mitochondrial membrane at ER-mitochondrial contact sites.
KW - ER-mitochondrial contact
KW - Mitochondrial dynamics
KW - Mitochondrial membrane constriction
KW - ENDOPLASMIC-RETICULUM
KW - FISSION
U2 - 10.1016/j.biocel.2021.106101
DO - 10.1016/j.biocel.2021.106101
M3 - Article
C2 - 34695569
SN - 1357-2725
VL - 141
JO - International Journal of Biochemistry & Cell Biology
JF - International Journal of Biochemistry & Cell Biology
M1 - 106101
ER -