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The mitochondrial inner membrane protein Mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled‐coil‐helix coiled‐coil‐helix domain‐containing protein 3 and 6 and DnaJC11
Author(s) -
Xie Jing,
Marusich Michael F.,
Souda Puneet,
Whitelegge Julian,
Capaldi Roderick A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.052
Subject(s) - inner mitochondrial membrane , coiled coil , microbiology and biotechnology , mitochondrial membrane transport protein , mitochondrion , translocase of the inner membrane , biology , inner membrane , mitochondrial carrier , chaperone (clinical) , membrane protein , bacterial outer membrane , biochemistry , membrane , gene , medicine , escherichia coli , pathology
A monoclonal antibody (mAb) has been produced which reacts with human mitofilin, a mitochondrial inner membrane protein. This mAb immunocaptures its target protein in association with six other proteins, metaxins 1 and 2, SAM50, CHCHD3, CHCHD6 and DnaJC11, respectively. The first three are outer membrane proteins, CHCHD3 has been assigned to the matrix space, and the other two proteins have not been described in mitochondria previously. The functional role of this new complex is uncertain. However, a role in protein import related to maintenance of mitochondrial structure is suggested as mitofilin helps regulate mitochondrial morphology and at least four of the associated proteins (metaxins 1 and 2, SAM50 and CHCHD3) have been implicated in protein import, while DnaJC11 is a chaperone‐like protein that may have a similar role.