| 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 |
| Page(s): | 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. |
| URI: | https://digitalcollection.zhaw.ch/handle/11475/6808 |
| 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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Schweizer, A., Stahl, P. D., & Rohrer, J. (2000). A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting. Journal of Biological Chemistry, 275(38), 29694–29700. https://doi.org/10.1074/jbc.M000571200
Schweizer, A., Stahl, P.D. and Rohrer, J. (2000) ‘A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting’, Journal of Biological Chemistry, 275(38), pp. 29694–29700. Available at: https://doi.org/10.1074/jbc.M000571200.
A. Schweizer, P. D. Stahl, and J. Rohrer, “A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting,” Journal of Biological Chemistry, vol. 275, no. 38, pp. 29694–29700, Sep. 2000, doi: 10.1074/jbc.M000571200.
SCHWEIZER, Anja, Philip D. STAHL und Jack ROHRER, 2000. A di-aromatic motif in the cytosolic tail of the mannose receptor mediates endosomal sorting. Journal of Biological Chemistry. 22 September 2000. Bd. 275, Nr. 38, S. 29694–29700. DOI 10.1074/jbc.M000571200
Schweizer, Anja, Philip D. Stahl, and Jack Rohrer. 2000. “A Di-Aromatic Motif in the Cytosolic Tail of the Mannose Receptor Mediates Endosomal Sorting.” Journal of Biological Chemistry 275 (38): 29694–700. https://doi.org/10.1074/jbc.M000571200.
Schweizer, Anja, et al. “A Di-Aromatic Motif in the Cytosolic Tail of the Mannose Receptor Mediates Endosomal Sorting.” Journal of Biological Chemistry, vol. 275, no. 38, Sept. 2000, pp. 29694–700, https://doi.org/10.1074/jbc.M000571200.
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