scholarly journals Armadillo repeat-containing protein 1 is a dual localization protein associated with mitochondrial intermembrane space bridging complex

2019 ◽  
Author(s):  
Fabienne Wagner ◽  
Tobias C. Kunz ◽  
Suvagata R. Chowdhury ◽  
Bernd Thiede ◽  
Martin Fraunholz ◽  
...  
Keyword(s):  
Intermembrane Space ◽  
Large Protein ◽  
Contact Site ◽  
Cellular Processes ◽  
Large Protein Complex ◽  
Dual Localization ◽  
Mammalian Mitochondria ◽  
Mitochondrial Distribution ◽  
Mitochondrial Intermembrane Space ◽  
Armadillo Repeat

AbstractCristae architecture is important for the function of mitochondria, the organelles that play the central role in many cellular processes. The mitochondrial contact site and cristae organizing system (MICOS) together with the sorting and assembly machinery (SAM) forms the mitochondrial intermembrane space bridging complex (MIB), a large protein complex present in mammalian mitochondria that partakes in the formation and maintenance of cristae. We report here a new subunit of the mammalian MICOS/MIB complex, an armadillo repeat-containing protein 1 (ArmC1). ArmC1 localizes both to cytosol and mitochondria, where it associates with the outer mitochondrial membrane through its carboxy-terminus. ArmC1 interacts with other constituents of the MICOS/MIB complex and its amounts are reduced upon MICOS/MIB complex depletion. Mitochondria lacking ArmC1 do not show defects in cristae structure, respiration or protein content, but appear fragmented and with reduced motility. ArmC1 represents therefore a peripheral MICOS/MIB component that appears to play a role in mitochondrial distribution in the cell.

scholarly journals Armadillo repeat-containing protein 1 is a dual localization protein associated with mitochondrial intermembrane space bridging complex

PLoS ONE ◽  
2019 ◽  
Vol 14 (10) ◽  
pp. e0218303 ◽  
Author(s):  
Fabienne Wagner ◽  
Tobias C. Kunz ◽  
Suvagata R. Chowdhury ◽  
Bernd Thiede ◽  
Martin Fraunholz ◽  
...  
Keyword(s):  
Intermembrane Space ◽  
Dual Localization ◽  
Mitochondrial Intermembrane Space ◽  
Armadillo Repeat

scholarly journals Uniform nomenclature for the mitochondrial contact site and cristae organizing system

2014 ◽  
Vol 204 (7) ◽  
pp. 1083-1086 ◽  
Author(s):  
Nikolaus Pfanner ◽  
Martin van der Laan ◽  
Paolo Amati ◽  
Roderick A. Capaldi ◽  
Amy A. Caudy ◽  
...  
Keyword(s):  
Large Protein ◽  
Contact Site ◽  
Inner Membrane ◽  
Future Studies ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Mitochondrial Inner Membrane ◽  
Large Protein Complex ◽  
Membrane Contact ◽  
Uniform Nomenclature

The mitochondrial inner membrane contains a large protein complex that functions in inner membrane organization and formation of membrane contact sites. The complex was variably named the mitochondrial contact site complex, mitochondrial inner membrane organizing system, mitochondrial organizing structure, or Mitofilin/Fcj1 complex. To facilitate future studies, we propose to unify the nomenclature and term the complex “mitochondrial contact site and cristae organizing system” and its subunits Mic10 to Mic60.

Mechanisms and physiological impact of the dual localization of mitochondrial intermembrane space proteins

2014 ◽  
Vol 42 (4) ◽  
pp. 952-958 ◽  
Author(s):  
Carmelina Petrungaro ◽  
Jan Riemer
Keyword(s):  
Oxidative Stress ◽  
Mitochondrial Function ◽  
The Other ◽  
Yeast Cells ◽  
Eukaryotic Cells ◽  
Intermembrane Space ◽  
Dual Localization ◽  
Mitochondrial Intermembrane Space ◽  
Physiological Impact ◽  
Cellular Compartments

Eukaryotic cells developed diverse mechanisms to guide proteins to more than one destination within the cell. Recently, the proteome of the IMS (intermembrane space) of mitochondria of yeast cells was identified showing that approximately 20% of all soluble IMS proteins are dually localized to the IMS, as well as to other cellular compartments. Half of these dually localized proteins are important for oxidative stress defence and the other half are involved in energy homoeostasis. In the present review, we discuss the mechanisms leading to the dual localization of IMS proteins and the implications for mitochondrial function.

scholarly journals Bid-Cardiolipin Interaction at Mitochondrial Contact Site Contributes to Mitochondrial Cristae Reorganization and Cytochrome c Release

2004 ◽  
Vol 15 (7) ◽  
pp. 3061-3072 ◽  
Author(s):  
Tae-Hyoung Kim ◽  
Yongge Zhao ◽  
Wen-Xing Ding ◽  
Jin Na Shin ◽  
Xi He ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Intermembrane Space ◽  
Mitochondrial Localization ◽  
Contact Site ◽  
Helical Structures ◽  
Cytochrome C Release ◽  
Outer Membranes ◽  
Bh3 Domain ◽  
Family Protein ◽  
Mitochondrial Intermembrane Space

Release of cytochrome c from the mitochondrial intermembrane space is critical to apoptosis induced by a variety of death stimuli. Bid is a BH3-only prodeath Bcl-2 family protein that can potently activate this efflux. In the current study, we investigated the mitochondrial localization of Bid and its interactions with mitochondrial phospholipids, focusing on their relationships with Bid-induced cytochrome c release. We found that Bid binding to the mitochondria required only three of its eight helical structures (α4-α6), but not the BH3 domain, and the binding could not be inhibited by the antideath molecule Bcl-xL. Membrane fractionations indicated that tBid bound to mitochondrial outer membranes at both contact and noncontact sites. Bid could interact with specific cardiolipin species on intact mitochondria as identified by mass spectrometry. Like the binding to the mitochondria, this interaction could not be blocked by the mutation in the BH3 domain or by Bcl-xL. However, a cardiolipin-specific dye, 10-N-nonyl acridine orange, could preferentially suppress Bid binding to the mitochondrial contact site and inhibit Bid-induced mitochondrial cristae reorganization and cytochrome c release. These findings thus suggest that interactions of Bid with mitochondrial cardiolipin at the contact site can contribute significantly to its functions.

scholarly journals Proteomic Mapping of the Human Mitochondrial Intermembrane Space in Live Cells via Ratiometric APEX Tagging

2014 ◽  
Vol 55 (2) ◽  
pp. 332-341 ◽  
Author(s):  
Victoria Hung ◽  
Peng Zou ◽  
Hyun-Woo Rhee ◽  
Namrata D. Udeshi ◽  
Valentin Cracan ◽  
...  
Keyword(s):  
Live Cells ◽  
Intermembrane Space ◽  
Mitochondrial Intermembrane Space
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