ABCMdb

PMID: 22045812

Hillebrand M, Gersting SW, Lotz-Havla AS, Schafer A, Rosewich H, Valerius O, Muntau AC, Gartner J
Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane.
J Biol Chem. 2012 Jan 2;287(1):210-21. Epub 2011 Nov 1., [PubMed]

Sentences

No. Mutations Sentence Comment

227 ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn ABCD1 p.Gly607Asp We analyzed, whether five missense mutations in the ABCD1 gene known to be associated with near normal ALDP protein amounts (G116R, S514N, G607D, G629H, and T693M) would induce edgetic perturbations by altering ALDP homo-oligomerization or the interaction of ALDP with FASN, ACLY, or FATP4 (Fig. 5). Login to comment 228 ABCD1 p.Ser514Asn Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization. Login to comment 229 ABCD1 p.Gly116Arg ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn ABCD1 p.Ser514Asn ABCD1 p.Gly607Asp Conversely, S514N and G607D increased the BRET ratio for the interaction of ALDP with FASN, whereas G116R had the same effect on the interaction between ALDP and ACLY. Login to comment 230 ABCD1 p.Ser514Asn Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization. Login to comment 231 ABCD1 p.Gly116Arg ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn ABCD1 p.Ser514Asn ABCD1 p.Gly607Asp We analyzed, whether five missense mutations in the ABCD1 gene known to be associated with near normal ALDP protein amounts (G116R, S514N, G607D, G629H, and T693M) would induce edgetic perturbations by altering ALDP homo-oligomerization or the interaction of ALDP with FASN, ACLY, or FATP4 (Fig. 5). Login to comment 232 ABCD1 p.Ser514Asn Two mutations, S514N and G629H, led to a reduction of the BRET ratio related to ALDP homo-oligomerization. Login to comment 233 ABCD1 p.Gly116Arg ABCD1 p.Ser514Asn Conversely, S514N and G607D increased the BRET ratio for the interaction of ALDP with FASN, whereas G116R had the same effect on the interaction between ALDP and ACLY. Login to comment 269 ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined. Login to comment 271 ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined. Login to comment 273 ABCD1 p.Gly116Arg ABCD1 p.Thr693Met ABCD1 p.Ser514Asn WT ALDP was compared with ALDP constructs representing disease-causing missense mutations (G116R, S514N, G607D, G629H, and T693M); homomeric interactions as well as interactions with FASN, ACLY, and FATP4 were determined. Login to comment 296 ABCD1 p.Gly116Arg ABCD1 p.Ser514Asn We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively. Login to comment 298 ABCD1 p.Gly116Arg ABCD1 p.Ser514Asn We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively. Login to comment 300 ABCD1 p.Gly116Arg ABCD1 p.Ser514Asn We showed that three of these mutations, G116R, S514N, and G607D, induced edgetic perturbations of PPI by exerting partly countervailing effects on ALDP homo-oligomerization and the interaction between ALDP and FASN and ALDP and ACLY, respectively. Login to comment