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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Biol+Chem
2014 ; 289
(17
): 11862-11872
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Transient contraction of mitochondria induces depolarization through the inner
membrane dynamin OPA1 protein
#MMPMID24627489
Lee H
; Yoon Y
J Biol Chem
2014[Apr]; 289
(17
): 11862-11872
PMID24627489
show ga
Dynamin-related membrane remodeling proteins regulate mitochondrial morphology by
mediating fission and fusion. Although mitochondrial morphology is considered an
important factor in maintaining mitochondrial function, a direct mechanistic link
between mitochondrial morphology and function has not been defined. We report
here a previously unrecognized cellular process of transient contraction of the
mitochondrial matrix. Importantly, we found that this transient morphological
contraction of mitochondria is accompanied by a reversible loss or decrease of
inner membrane potential. Fission deficiency greatly amplified this phenomenon,
which functionally exhibited an increase of inner membrane proton leak. We found
that electron transport activity is necessary for the morphological contraction
of mitochondria. Furthermore, we discovered that silencing the inner
membrane-associated dynamin optic atrophy 1 (OPA1) in fission deficiency
prevented mitochondrial depolarization and decreased proton leak without blocking
mitochondrial contraction, indicating that OPA1 is a factor in coupling matrix
contraction to mitochondrial depolarization. Our findings show that transient
matrix contraction is a novel cellular mechanism regulating mitochondrial
activity through the function of the inner membrane dynamin OPA1.