Peroxisome assembly factor 2 is a protein that in humans is encoded by the PEX6gene.[1][2] PEX6 is an AAA ATPase that localizes to the peroxisome. PEX6 forms a hexamer with PEX1[3][4] and is recruited to the membrane by PEX26.[5]
From yeast to plants to humans, there is only one verified function of PEX6; PEX6 (and PEX1) removes PEX5 from the peroxisomal membrane so that PEX5 may do additional rounds of peroxisomal import. Human PEX6 can genetically complement plant pex6 mutants, which highlights functional conservation.[6] Work with pex6 mutants in Arabidopsis thaliana has shown that PEX6 may have a role in consuming oil body (plant-specific lipid droplets).[7] Work with yeast pex6 mutants has shown that PEX6 is a key player in the autophagy of peroxisomes called pexophagy.[8]
↑Tamura S, Shimozawa N, Suzuki Y, Tsukamoto T, Osumi T, Fujiki Y (April 1998). "A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p". Biochemical and Biophysical Research Communications. 245 (3): 883–6. doi:10.1006/bbrc.1998.8522. PMID9588209.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Tamura S, Shimozawa N, Suzuki Y, Tsukamoto T, Osumi T, Fujiki Y (April 1998). "A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p". Biochemical and Biophysical Research Communications. 245 (3): 883–6. doi:10.1006/bbrc.1998.8522. PMID9588209.
Zhang Z, Suzuki Y, Shimozawa N, Fukuda S, Imamura A, Tsukamoto T, Osumi T, Fujiki Y, Orii T, Wanders RJ, Barth PG, Moser HW, Paton BC, Besley GT, Kondo N (1999). "Genomic structure and identification of 11 novel mutations of the PEX6 (peroxisome assembly factor-2) gene in patients with peroxisome biogenesis disorders". Human Mutation. 13 (6): 487–96. doi:10.1002/(SICI)1098-1004(1999)13:6<487::AID-HUMU9>3.0.CO;2-T. PMID10408779.
Matsumoto N, Tamura S, Moser A, Moser HW, Braverman N, Suzuki Y, Shimozawa N, Kondo N, Fujiki Y (2001). "The peroxin Pex6p gene is impaired in peroxisomal biogenesis disorders of complementation group 6". Journal of Human Genetics. 46 (5): 273–7. doi:10.1007/s100380170078. PMID11355018.
Matsumoto N, Tamura S, Fujiki Y (May 2003). "The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes". Nature Cell Biology. 5 (5): 454–60. doi:10.1038/ncb982. PMID12717447.
Warner DR, Roberts EA, Greene RM, Pisano MM (December 2003). "Identification of novel Smad binding proteins". Biochemical and Biophysical Research Communications. 312 (4): 1185–90. doi:10.1016/j.bbrc.2003.11.049. PMID14651998.
Furuki S, Tamura S, Matsumoto N, Miyata N, Moser A, Moser HW, Fujiki Y (January 2006). "Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with the Pex1p x Pex6p complex". The Journal of Biological Chemistry. 281 (3): 1317–23. doi:10.1074/jbc.M510044200. PMID16257970.
Tamura S, Yasutake S, Matsumoto N, Fujiki Y (September 2006). "Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p". The Journal of Biological Chemistry. 281 (38): 27693–704. doi:10.1074/jbc.M605159200. PMID16854980.