Mitofilin and the Mitochondrial Inner Membrane Organizing System (MINOS)

Fri, 11/30/2012 - 11:55

Mitofilin was originally described as a heart muscle protein due to its high expression in the heart. Recently, analysis of the human heart mitochondrial proteome demonstrated that Mitofilin is one of the most abundant mitochondrial proteins (1). Researchers have reported finding two alternately spliced Mitofilin variants producing proteins of 88 and 90 kDa, that were detected in immunoblots with Mitofilin antibodies (2).

IF analysis of Mitofilin in HeLa cells.

Mitofilin is part of a large inner membrane complex, and has five partner proteins as constituents of the mitochondrial inner membrane organizing system (MINOS) that is required for keeping cristae membranes connected to the inner boundary membrane. Mitofilin is a central component of MINOS and functions as a multifunctional regulator of mitochondrial architecture and protein biogenesis (3). Mitochondria amplify caspase-dependent apoptosis by releasing proapoptotic proteins, especially Cytochrome C. Recent studies demonstrated that Mitofilin acts as a cristae controller to regulate Cytochrome C release during apoptosis. Knockdown of Mitofilin with RNAi led to fragmentation of the mitochondrial network and disorganization of the cristae, suggesting a potential role for Mitofilin in cristae remodeling and controlling Cytochrome C release during apoptosis (4).

  1. PMID: 12592411
  2. PMID: 9168817
  3. PMID: 21944719
  4. PMID: 23058921

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