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Gimap3

A foot-in-the-door to tissue-specific regulation of mitochondrial DNA genetics

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Pages 31-35 | Received 06 Dec 2010, Accepted 23 Jan 2011, Published online: 01 Jan 2011

Figures & data

Figure 1 Gimap3 protein variation in mice. (A) Schematic of BALB/c and CAST/Ei Gimap3 variants with an AIG domain, coiled-coil (CC) and transmembrane domain (TM). The AIG domain consists of a G1–G5 GTPase domain and a hydrophobic conserved box located between G3 and G4. BALB and CAST Gimap3 variants are identical in sequence except at the N-terminus due to differential splicing resulting in an additional 58 amino acids in the CAST form. All common laboratory mouse strains (Mus mus domesticus) have the BALB variant of Gimap3. (B) Amino acid sequence alignment at the N-terminus of BALB and CAST Gimap3. Black boxes indicate regions of identity and the beginning of the AIG domain is indicated.

Figure 1 Gimap3 protein variation in mice. (A) Schematic of BALB/c and CAST/Ei Gimap3 variants with an AIG domain, coiled-coil (CC) and transmembrane domain (TM). The AIG domain consists of a G1–G5 GTPase domain and a hydrophobic conserved box located between G3 and G4. BALB and CAST Gimap3 variants are identical in sequence except at the N-terminus due to differential splicing resulting in an additional 58 amino acids in the CAST form. All common laboratory mouse strains (Mus mus domesticus) have the BALB variant of Gimap3. (B) Amino acid sequence alignment at the N-terminus of BALB and CAST Gimap3. Black boxes indicate regions of identity and the beginning of the AIG domain is indicated.

Figure 2 Possible models for selecting mitochondrial DNA (mtDNA) haplotypes in leukocytes and the potential role of Gimap3. (A) MtDNA selection is due to intracellular organelle selection resulting from the export of NZB-encoded mitochondrial peptides. Mitochondrially-encoded fMet peptides are known to be exported from mitochondria and form the basis of the maternally-transmitted antigen. Gimap3 could function in the export or recognition of mitochondrially-encoded peptides. (B) MtDNA selection is due to mitochondrially-derived vesicles. Vesicles are known to bud off from mitochondria. Gimap3 could function in the biogenesis or recognition of vesicles.

Figure 2 Possible models for selecting mitochondrial DNA (mtDNA) haplotypes in leukocytes and the potential role of Gimap3. (A) MtDNA selection is due to intracellular organelle selection resulting from the export of NZB-encoded mitochondrial peptides. Mitochondrially-encoded fMet peptides are known to be exported from mitochondria and form the basis of the maternally-transmitted antigen. Gimap3 could function in the export or recognition of mitochondrially-encoded peptides. (B) MtDNA selection is due to mitochondrially-derived vesicles. Vesicles are known to bud off from mitochondria. Gimap3 could function in the biogenesis or recognition of vesicles.