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J Biol Chem, Vol. 274, Issue 46, 32738-32743, November 12, 1999
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From the Mammalian peroxisomal proteins
adrenoleukodystrophy protein (ALDP), adrenoleukodystrophy-related
protein (ALDRP), and 70-kDa peroxisomal protein (PMP70) belong to the
superfamily of ATP-binding cassette (ABC) transporters. Unlike many ABC
transporters that are single functional proteins with two related
halves, ALDP, ALDRP, and PMP70 have the structure of ABC
half-transporters. The dysfunction of ALDP is responsible for X-linked
adrenoleukodystrophy (X-ALD), a neurodegenerative disorder in which
saturated very long-chain fatty acids accumulate because of their
impaired peroxisomal INSERM U342, Institut Cochin de
Génétique Moléculaire, Hôpital
Saint-Vincent-de-Paul, 82 Avenue Denfert Rochereau,
75014 Paris, France and ¶ Institut Cochin de
Génétique Moléculaire, EPI 9923, INSERM,
Université Paris V, 24 Rue du Faubourg Saint-Jacques,
75014 Paris France
-oxidation. No disease has so far been
associated with mutations of adrenoleukodystrophy-related or PMP70
genes. It has been proposed that peroxisomal ABC transporters need to
dimerize to exert import functions. Using the yeast two-hybrid system,
we show that homo- as well as heterodimerization occur between the
carboxyl-terminal halves of ALDP, ALDRP, and PMP70. Two X-ALD disease
mutations located in the carboxyl-terminal half of ALDP affect both
homo- and heterodimerization of ALDP. Co-immunoprecipitation
demonstrated the homodimerization of ALDP, the heterodimerization of
ALDP with PMP70 or ALDRP, and the heterodimerization of ALDRP with
PMP70. These results provide the first evidence of both homo- and
heterodimerization of mammalian ABC half-transporters and suggest that
the loss of ALDP dimerization plays a role in X-ALD pathogenesis.
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