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J. Biol. Chem., Vol. 277, Issue 42, 40142-40147, October 18, 2002

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ATP Binding/Hydrolysis by and Phosphorylation of Peroxisomal ATP-binding Cassette Proteins PMP70 (ABCD3) and Adrenoleukodystrophy Protein (ABCD1)^*

Arowu R. Tanaka^§, Kouichi Tanabe^§, Masashi Morita^¶, Mikinori Kurisu^¶, Yoshinori Kasiwayama^¶, Michinori Matsuo, Noriyuki Kioka, Teruo Amachi, Tsuneo Imanaka^¶, and Kazumitsu Ueda

From the  Laboratory of Cellular Biochemistry, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan and ^¶ Department of Biological Chemistry, Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, 2630 Sugitani, Toyama 930-0194, Japan

The 70-kDa peroxisomal membrane protein (PMP70) and adrenoleukodystrophy protein (ALDP), half-size ATP-binding cassette transporters, are involved in metabolic transport of long and very long chain fatty acids into peroxisomes. We examined the interaction of peroxisomal ATP-binding cassette transporters with ATP using rat liver peroxisomes. PMP70 was photoaffinity-labeled at similar efficiencies with 8-azido-[-³²P]ATP and 8-azido-[-³²P]ATP when peroxisomes were incubated with these nucleotides at 37 °C in the absence Mg²⁺ and exposed to UV light without removing unbound nucleotides. The photoaffinity-labeled PMP70 and ALDP were co-immunoprecipitated together with other peroxisomal proteins, which also showed tight ATP binding properties. Addition of Mg²⁺ reduced the photoaffinity labeling of PMP70 with 8-azido-[-³²P]ATP by 70%, whereas it reduced photoaffinity labeling with 8-azido-[-³²P]ATP by only 20%. However, two-thirds of nucleotide (probably ADP) was dissociated during removal of unbound nucleotides. These results suggest that ATP binds to PMP70 tightly in the absence of Mg²⁺, the bound ATP is hydrolyzed to ADP in the presence of Mg²⁺, and the produced ADP is dissociated from PMP70, which allows ATP hydrolysis turnover. Properties of photoaffinity labeling of ALDP were essentially similar to those of PMP70. Vanadate-induced nucleotide trapping in PMP70 and ALDP was not observed. PMP70 and ALDP were also phosphorylated at a tyrosine residue(s). ATP binding/hydrolysis by and phosphorylation of PMP70 and ALDP are involved in the regulation of fatty acid transport into peroxisomes.

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