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Title

Trichoplein/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition

Authors
Cerqua, Cristina
Anesti, Vassiliki
Naon, Deborah
Wiche, Gerhard
Baffa, Raffaele
Dimmer, Kai S.
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Published in EMBO Reports. 2010, vol. 11, no. 11, p. 854-860
Abstract Trichoplein/mitostatin (TpMs) is a keratin-binding protein that partly colocalizes with mitochondria and is often downregulated in epithelial cancers, but its function remains unclear. In this study, we report that TpMs regulates the tethering between mitochondria and endoplasmic reticulum (ER) in a Mitofusin 2 (Mfn2)-dependent manner. Subcellular fractionation and immunostaining show that TpMs is present at the interface between mitochondria and ER. The expression of TpMs leads to mitochondrial fragmentation and loosens tethering with ER, whereas its silencing has opposite effects. Functionally, the reduced tethering by TpMs inhibits apoptosis by Ca(2+)-dependent stimuli that require ER-mitochondria juxtaposition. Biochemical and genetic evidence support a model in which TpMs requires Mfn2 to modulate mitochondrial shape and tethering. Thus, TpMs is a new regulator of mitochondria-ER juxtaposition.
Keywords AnimalsCalcium/pharmacologyCarrier Proteins/*metabolismCell Death/drug effectsEndoplasmic Reticulum/drug effects/*metabolismGTP Phosphohydrolases/metabolismHeLa CellsHumansMembrane Proteins/metabolismMiceMitochondria/drug effects/*metabolismMitochondrial Proteins/metabolismOrganelle Shape/drug effectsProtein Binding/drug effectsProtein Transport/drug effectsTumor Suppressor Proteins/*metabolism
Identifiers
PMID: 20930847
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Structures
Research group Les mitochondries dans la vie cellulaire (850)
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CERQUA, Cristina et al. Trichoplein/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition. In: EMBO Reports, 2010, vol. 11, n° 11, p. 854-860. https://archive-ouverte.unige.ch/unige:20833

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Deposited on : 2012-05-23

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