ABCMdb

PMID: 11274200

Harris MJ, Kuwano M, Webb M, Board PG
Identification of the apical membrane-targeting signal of the multidrug resistance-associated protein 2 (MRP2/MOAT).
J Biol Chem. 2001 Jun 15;276(24):20876-81. Epub 2001 Mar 27., [PubMed]

Sentences

No. Mutations Sentence Comment

97 ABCC2 p.Thr1543Ala ABCC2 p.Lys1544Ala The T1543A and K1544A mutants had both apical and basolateral targeting (nonpolarized distribution) with an increase in protein accumulation in intracellular vesicles. Login to comment 98 ABCC2 p.Phe1545Ala The F1545A mutant did not have altered targeting. Login to comment 109 ABCC2 p.Thr1543Ala A, the T1543A mutation produced a nonpolarized distribution of the fusion protein. Login to comment 112 ABCC2 p.Lys1544Ala B, the K1544A mutation also lost polarized distribution of the protein with the protein detected in the apical and basolateral membranes. Login to comment 113 ABCC2 p.Phe1545Ala C, F1545A, mutation of the C-terminal residue to alanine, did not alter the apical targeting of the protein. Login to comment 115 ABCC2 p.Ser1542Ala E, S1542A, mutation of the serine produced a less distinct distribution. Login to comment 162 ABCC2 p.Thr1543Ala The T1543A mutant did produce a change in targeting compared with the native protein, allowing both basolateral and apical targeting, i.e. nonpolarized targeting, and also an increased accumulation in vesicles, suggesting some instability in the targeting mechanism. Login to comment 165 ABCC2 p.Phe1545Ala The F1545A mutant did not alter normal targeting, suggesting that alanine is a sufficiently hydrophobic residue. Login to comment 166 ABCC2 p.Lys1544Ala The canonical PDZ domain is reported to tolerate any residue (X) at the -1 position, but the K1544A caused nonpolarized targeting, suggesting some flexibility in the constraints determining functional PDZ domains. Login to comment