Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting
Authors: Schweizer, Anja
Stahl, Philip D.
Rohrer, Jack
DOI: 10.1074/jbc.M000571200
Published in: Journal of Biological Chemistry
Volume(Issue): 275
Issue: 38
Pages: 29694
Pages to: 29700
Issue Date: 22-Sep-2000
Publisher / Ed. Institution: American Society for Biochemistry and Molecular Biology
ISSN: 1083-351X
Language: English
Subject (DDC): 571: Physiology and related subjects
572: Biochemistry
Abstract: The mannose receptor (MR), the prototype of a new family of multilectin receptor proteins important in innate immunity, undergoes rapid internalization and recycling from the endosomal system back to the cell surface. Sorting of the MR in endosomes prevents the receptor from entering lysosomes where it would be degraded. Here, we focused on a diaromatic sequence (Tyr(18)-Phe(19)) in the MR cytoplasmic tail as an endosomal sorting signal. The subcellular distribution of chimeric constructs between the MR and the cation-dependent mannose 6-phosphate receptor was assessed by Percoll density gradients and cell surface assays. Unlike the wild type constructs, mutant receptors with alanine substitutions of Tyr(18)-Phe(19) were highly missorted to lysosomes, indicating that the di-aromatic motif of the MR cytoplasmic tail mediates sorting in endosomes. Within this sequence Tyr(18) is the key residue with Phe(19) contributing to this function. Moreover, Tyr(18) was also found to be essential for internalization, consistent with the presence of overlapping signals for internalization and endosomal sorting in the cytosolic tail of the MR. A di-aromatic amino acid sequence in the cytosolic tail has now been shown to function in two receptors known to be internalized from the plasma membrane, the MR and the cation-dependent mannose 6-phosphate receptor. This feature therefore appears to be a general determinant for endosomal sorting.
Fulltext version: Published version
License (according to publishing contract): Licence according to publishing contract
Departement: Life Sciences and Facility Management
Appears in Collections:Publikationen Life Sciences und Facility Management

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