نتایج جستجو برای: Mitofilin

تعداد نتایج: 68  

Journal: :Developmental cell 2011
Karina von der Malsburg Judith M Müller Maria Bohnert Silke Oeljeklaus Paulina Kwiatkowska Thomas Becker Adrianna Loniewska-Lwowska Sebastian Wiese Sanjana Rao Dusanka Milenkovic Dana P Hutu Ralf M Zerbes Agnes Schulze-Specking Helmut E Meyer Jean-Claude Martinou Sabine Rospert Peter Rehling Chris Meisinger Marten Veenhuis Bettina Warscheid Ida J van der Klei Nikolaus Pfanner Agnieszka Chacinska Martin van der Laan

The mitochondrial inner membrane consists of two domains, inner boundary membrane and cristae membrane that are connected by crista junctions. Mitofilin/Fcj1 was reported to be involved in formation of crista junctions, however, different views exist on its function and possible partner proteins. We report that mitofilin plays a dual role. Mitofilin is part of a large inner membrane complex, an...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2010
Young-Un Park Jaehoon Jeong Haeryun Lee Ji Young Mun Joung-Hun Kim Jong Seo Lee Minh Dang Nguyen Sung Sik Han Pann-Ghill Suh Sang Ki Park

Disrupted-in-schizophrenia 1 (DISC1) has emerged as a schizophrenia-susceptibility gene affecting various neuronal functions. In this study, we characterized Mitofilin, a mitochondrial inner membrane protein, as a mediator of the mitochondrial function of DISC1. A fraction of DISC1 was localized to the inside of mitochondria and directly interacts with Mitofilin. A reduction in DISC1 function i...

Journal: :Journal of cell science 1996
P R Odgren G Toukatly P L Bangs R Gilmore E G Fey

We have identified and characterized a human protein of the mitochondria which we call mitofilin. Using monoclonal and polyclonal antibodies, we have isolated cDNA clones and characterized mitofilin biochemically. It appears as a 90 and 91 kDa doublet in western blots and is translated from a single 2.7 kb mRNA. Antibodies raised against cellular and bacterially-expressed protein given identica...

2015
Chengli Ding Zhifei Wu Lei Huang Yajie Wang Jie Xue Si Chen Zixin Deng Lianrong Wang Zhiyin Song Shi Chen

The inner mitochondrial membrane (IMM) invaginates to form cristae and the maintenance of cristae depends on the mitochondrial contact site (MICOS) complex. Mitofilin and CHCHD6, which physically interact, are two components of the MICOS. In this study, we performed immunoprecipitation experiments with Mitofilin and CHCHD6 antibodies and identified a complex containing Mitofilin, Sam50, and CHC...

Journal: :Molecular biology of the cell 2005
George B John Yonglei Shang Li Li Christian Renken Carmen A Mannella Jeanne M L Selker Linda Rangell Michael J Bennett Jiping Zha

Mitochondria are complex organelles with a highly dynamic distribution and internal organization. Here, we demonstrate that mitofilin, a previously identified mitochondrial protein of unknown function, controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into ...

Objective(s): Mitofilin contributes to the maintenance of mitochondrial structure and functions. This study was undertaken to determine the mechanisms underlying its regulation of apoptosis.  Materials and Methods: Mitofilin was knockdowned by specific short hairpin RNA (shRNA) and the stable HeLa cell clone was selected. The autophagy a...

2017
Manuel Hessenberger Ralf M Zerbes Heike Rampelt Séverine Kunz Audrey H Xavier Bettina Purfürst Hauke Lilie Nikolaus Pfanner Martin van der Laan Oliver Daumke

The mitochondrial contact site and cristae organizing system (MICOS) is crucial for the formation of crista junctions and mitochondrial inner membrane architecture. MICOS contains two core components. Mic10 shows membrane-bending activity, whereas Mic60 (mitofilin) forms contact sites between inner and outer membranes. Here we report that Mic60 deforms liposomes into thin membrane tubules and t...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2013
Daniel C Jans Christian A Wurm Dietmar Riedel Dirk Wenzel Franziska Stagge Markus Deckers Peter Rehling Stefan Jakobs

The mitochondrial inner membrane organizing system (MINOS) is a conserved large hetero-oligomeric protein complex in the mitochondrial inner membrane, crucial for the maintenance of cristae morphology. MINOS has been suggested to represent the core of an extended protein network that controls mitochondrial function and structure, and has been linked to several human diseases. The spatial arrang...

2013
Tobias A. Weber Sebastian Koob Heinrich Heide Ilka Wittig Brian Head Alexander van der Bliek Ulrich Brandt Michel Mittelbronn Andreas S. Reichert

Mitochondrial cristae morphology is highly variable and altered under numerous pathological conditions. The protein complexes involved are largely unknown or only insufficiently characterized. Using complexome profiling we identified apolipoprotein O (APOO) and apolipoprotein O-like protein (APOOL) as putative components of the Mitofilin/MINOS protein complex which was recently implicated in de...

2012
Maria Bohnert Lena-Sophie Wenz Ralf M. Zerbes Susanne E. Horvath David A. Stroud Karina von der Malsburg Judith M. Müller Silke Oeljeklaus Inge Perschil Bettina Warscheid Agnieszka Chacinska Marten Veenhuis Ida J. van der Klei Günther Daum Nils Wiedemann Thomas Becker Nikolaus Pfanner Martin van der Laan

Mitochondria contain two membranes, the outer membrane and the inner membrane with folded cristae. The mitochondrial inner membrane organizing system (MINOS) is a large protein complex required for maintaining inner membrane architecture. MINOS interacts with both preprotein transport machineries of the outer membrane, the translocase of the outer membrane (TOM) and the sorting and assembly mac...

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