2002年10月
ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)
JOURNAL OF BIOLOGICAL CHEMISTRY
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- 巻
- 277
- 号
- 42
- 開始ページ
- 40142
- 終了ページ
- 40147
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1074/jbc.M205079200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
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-[alpha-P-32]ATP and 8-azido-[gamma-P-32]ATp when peroxisomes were incubated with these nucleotides at 37 degreesC 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-[gamma-P-32]ATp by 70%, whereas it reduced photoaffinity labeling with 8-azido-[alpha-P-32]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.
- リンク情報
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- DOI
- https://doi.org/10.1074/jbc.M205079200
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902145134533242
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/12176987
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000178662500137&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1074/jbc.M205079200
- ISSN : 0021-9258
- J-Global ID : 200902145134533242
- PubMed ID : 12176987
- Web of Science ID : WOS:000178662500137