Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosis

Mostov, Keith E.; Kops, Anne de Bruyn; Deitcher, David L.

doi:10.1016/0092-8674(86)90592-1

Cited by 194 publications

(82 citation statements)

References 26 publications

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“…It has been demonstrated, using density shift procedures, that two co-internalised ligands, one of which recycles, are found in different compartments at very early time points after internalisation (Stoorvogel et al, 1987). Similarly, Mueller and Hubbard (1986), by using '251-labelling, were able to define two populations of endosomes from rat liver one of which contained both asialoglycoprotein receptor (a recycling receptor) and its ligand, asialoorosomucoid, and the other which contained the ligand alone. The receptor-positive endosomes were similar morphologically to 'early' endosomes and in a perfusion experiment were first to be labelled with ligand while the receptor-negative structures contained multivesicular bodies and only later became labelled by ligand.…”

Section: Acid Sortingmentioning

confidence: 92%

The mechanism of receptor‐mediated endocytosis

Smythe

Warren

1991

European Journal of Biochemistry

153

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Section: Acid Sortingmentioning

confidence: 92%

The mechanism of receptor‐mediated endocytosis

Smythe

Warren

1991

European Journal of Biochemistry

153

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“…Polarized MDCK cells expressing receptors were isolated and characterized as described (19,20). Two clones expressing the "pIgR R654stop" mutant, where all but two residues of the cytoplasmic tail have been deleted (47), have been isolated and their exocytic transport characteristics were analyzed and found to be identical to those described for the earlier characterized expressors (47). The pIgR-⌬ 655-668 mutant whose 15 of the 17 residues comprising the basolateral sorting signal have been deleted in-frame is delivered from the TGN directly to the apical surface (27).…”

Section: Characterization Of Mdck Cells Stably Expressing the Pigr-mdckmentioning

confidence: 99%

Interactions of the AP-1 Golgi Adaptor with the Polymeric Immunoglobulin Receptor and Their Possible Role in Mediating Brefeldin A-sensitive Basolateral Targeting from the trans-Golgi Network

Orzech

Schlessinger

Weiss

et al. 1999

Journal of Biological Chemistry

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We provide morphological, biochemical, and functional evidence suggesting that the AP-1 clathrin adaptor complex of the trans-Golgi network interacts with the polymeric immunoglobulin receptor in transfected Madin-Darby canine kidney cells. Our results indicate that immunofluorescently labeled ␥-adaptin subunit of the adaptor complex and the polymeric immunoglobulin receptor partially co-localize in polarized and semi-polarized cells. ␥-Adaptin is co-immunoisolated with membranes expressing the wild-type receptor. The entire AP-1 adaptor complex could be chemically cross-linked to the receptor in filter-grown cells. ␥-Adaptin could be co-immunoprecipitated with the wild-type receptor, with reduced efficiency with receptor mutant whose basolateral sorting motif has been deleted, and not with receptor lacking its cytoplasmic tail. Co-immunoprecipitation of ␥-adaptin was inhibited by brefeldin A. Mutation of cytoplasmic serine 726 inhibited receptor interactions with AP-1 but did not abrogate the fidelity of its basolateral targeting from the trans-Golgi network. However, the kinetics of receptor delivery to the basolateral cell surface were slowed by the mutation. Although surface delivery of the wild-type receptor was inhibited by brefeldin A, the delivery of the mutant receptor was insensitive to the drug. Our results are consistent with a working model in which phosphorylated cytoplasmic serine modulates the recruitment of the polymeric immunoglobulin receptor into AP-1/clathrincoated areas in the trans-Golgi network. This process may regulate the efficiency of receptor targeting from the trans-Golgi network.

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“…The eDNA encoding the pIgR was subcloned into the vector M13mp8 as described previously (Mostov et al, 1986). Unless otherwise mentioned, mutations were construeted using a mutant DNA generated by insertion of a stop codon instead of I"670 as a starting template.…”

Section: Generation Of Cell Lines Expressing Mutant Plgrsmentioning

confidence: 99%

Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor.

Aroeti

Kosen

Kuntz

et al. 1993

The Journal of Cell Biology

140

138

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Abstract. The 17-juxtamembrane cytoplasmic residues of the polymeric immunoglobulin receptor contain an autonomous basolateral targeting signal that does not mediate rapid endocytosis (Casanova, J. E., G. Apodaca, and K. E. . Alanine-scanning mutagenesis identifies three residues in this region, His656, Arg657, and Va1660, that are most essential for basolateral sorting and two residues, Arg655 and Tyr668, that play a lesser role in this process. Progressive truncations suggested that Ser664 and Ile665 might also play a role in basolateral sorting. However, mutation of these residues to Ala or internal deletions of these residues did not affect basolateral sorting, indicating that these residues are probably not required for basolateral sorting. Twodimensional NMR spectroscopy of a peptide corresponding to the 17-mer signal indicates that the sequence Arg658-Asn-Val-Asp661 has a propensity to adopt a/if-turn in solution. Residues COOH-terminal to the B-turn (Arg662 to Arg669) seem to take up a nascent helix structure in solution. Substitution of Va1660 with Ala destabilizes the turn, while mutation of Arg657 to Ala does not appear to affect the turn structure. Neither mutation detectably altered the stability of the nascent helix in the COOH-terminal portion of the peptide.p OLARIZED epithelial cells have two plasma membrane domains: the apical domain facing the external environment, and the basolateral domain facing the internal milieu. These domains display striking differences in protein and lipid composition (Caplan and Matlin, 1989;

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Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosis

Cited by 194 publications

References 26 publications

The mechanism of receptor‐mediated endocytosis

The mechanism of receptor‐mediated endocytosis

Interactions of the AP-1 Golgi Adaptor with the Polymeric Immunoglobulin Receptor and Their Possible Role in Mediating Brefeldin A-sensitive Basolateral Targeting from the trans-Golgi Network

Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor.

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