PMID- 10551832
OWN - NLM
STAT- MEDLINE
DCOM- 20000103
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 46
DP  - 1999 Nov 12
TI  - Homo- and heterodimerization of peroxisomal ATP-binding cassette
      half-transporters.
PG  - 32738-43
AB  - 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 beta-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.
FAU - Liu, L X
AU  - Liu LX
AD  - INSERM U342, Institut Cochin de Genetique Moleculaire, Hopital
      Saint-Vincent-de-Paul, 82 Avenue Denfert Rochereau, 75014 Paris, France.
FAU - Janvier, K
AU  - Janvier K
FAU - Berteaux-Lecellier, V
AU  - Berteaux-Lecellier V
FAU - Cartier, N
AU  - Cartier N
FAU - Benarous, R
AU  - Benarous R
FAU - Aubourg, P
AU  - Aubourg P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (ABCD1 protein, human)
RN  - 0 (ABCD2 protein, human)
RN  - 0 (ABCD3 protein, human)
RN  - 0 (ATP Binding Cassette Transporter, Subfamily D)
RN  - 0 (ATP Binding Cassette Transporter, Subfamily D, Member 1)
RN  - 0 (ATP-Binding Cassette Transporters)
RN  - 0 (Abcd3 protein, mouse)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
SB  - IM
MH  - ATP Binding Cassette Transporter, Subfamily D
MH  - ATP Binding Cassette Transporter, Subfamily D, Member 1
MH  - ATP-Binding Cassette Transporters/*chemistry/genetics
MH  - Adrenoleukodystrophy/etiology/genetics
MH  - Animals
MH  - Dimerization
MH  - Humans
MH  - Membrane Proteins/*chemistry/genetics
MH  - Mice
MH  - Mutagenesis
MH  - Peroxisomes/*chemistry
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Proteins/*chemistry/genetics
MH  - Yeasts
EDAT- 1999/11/07 00:00
MHDA- 1999/11/07 00:01
CRDT- 1999/11/07 00:00
PHST- 1999/11/07 00:00 [pubmed]
PHST- 1999/11/07 00:01 [medline]
PHST- 1999/11/07 00:00 [entrez]
AID - 10.1074/jbc.274.46.32738 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 12;274(46):32738-43. doi: 10.1074/jbc.274.46.32738.