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dc.contributor.authorOdgren, Paul R.
dc.contributor.authorToukatly, Gary
dc.contributor.authorBangs, Peter Lawrence
dc.contributor.authorGilmore, Reid
dc.contributor.authorFey, Edward G.
dc.date2022-08-11T08:09:02.000
dc.date.accessioned2022-08-23T16:16:09Z
dc.date.available2022-08-23T16:16:09Z
dc.date.issued1996-09-01
dc.date.submitted2008-11-24
dc.identifier.citation<p>J Cell Sci. 1996 Sep;109 ( Pt 9):2253-64.</p>
dc.identifier.issn0021-9533 (Print)
dc.identifier.pmid8886976
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34261
dc.description.abstractWe 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8886976&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttp://jcs.biologists.org/cgi/content/abstract/109/9/2253
dc.subjectActins; 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
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMolecular characterization of mitofilin (HMP), a mitochondria-associated protein with predicted coiled coil and intermembrane space targeting domains
dc.typeJournal Article
dc.source.journaltitleJournal of cell science
dc.source.volume109 ( Pt 9)
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/916
dc.identifier.contextkey671846
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/916
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages2253-64


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