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    Molecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains

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    Authors
    Odgren, Paul R.
    Toukatly, Gary
    Bangs, Peter Lawrence
    Gilmore, Reid
    Fey, Edward G.
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Department of Cell Biology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    1996-09-01
    Keywords
    Actins; Amino Acid Sequence; Animals; Antibodies; Binding Sites; Cell Line; Cloning, Molecular; DNA, Complementary; Detergents; Humans; Mice; Microscopy, Fluorescence; Microscopy, Immunoelectron; Microtubules; Mitochondria; Mitochondrial Proteins; Molecular Sequence Data; Molecular Structure; Muscle Proteins; RNA, Messenger; Recombinant Fusion Proteins
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://jcs.biologists.org/cgi/content/abstract/109/9/2253
    Abstract
    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 identical cytoplasmic immunofluorescence and immunoblot results. Mitofilin co-localizes with mitochondria in immunofluorescence experiments and co-purifies with mitochondria. Double label studies show co-localization only with mitochondria and not with Golgi or endoplasmic reticulum. Co-localization with mitochondria is retained when actin or tubulin are de-polymerized, and mitofilin is expressed in all human cell types tested. The cDNA encodes a polypeptide with a central alpha-helical region with predicted coiled coil domains flanked by globular amino and carboxy termini. Unlike coiled coil motor proteins, mitofilin is resistant to detergent extraction. The presence of mitochondrial targeting and stop-transfer sequences, along with the accessibility of mitofilin to limited proteolysis suggests that it resides predominantly in the intermembrane space, consistent with immuno-electron micrographs which show mitofilin mainly at the mitochondrial periphery. The cDNA sequence of mitofilin is identical to that recently reported by Icho et al. (1994; Gene 144, 301-306) for a mRNA preferentially expressed in heart muscle (HMP), consistent with the high levels of mitochondria in cardiac myocytes.
    Source

    J Cell Sci. 1996 Sep;109 ( Pt 9):2253-64.

    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/34261
    PubMed ID
    8886976
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