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A chimera of the cytoplasmic tail of the mannose 6-phosphate/IGF-II receptor and lysozyme localizes to the TGN rather than prelysosomes where the bulk of the endogenous receptor is found.
- Source :
-
Journal of cell science [J Cell Sci] 1994 Apr; Vol. 107 ( Pt 4), pp. 923-32. - Publication Year :
- 1994
-
Abstract
- We fused the cytoplasmic and transmembrane domains of the bovine mannose 6-phosphate/IGF-II receptor (MPR) to lysozyme, a monomeric secretory protein thought to be devoid of sorting information. When the resulting chimera (lys/MPR) was transiently expressed in COS cells or stably expressed in CV1 cells, it had a predominantly intracellular distribution in the trans-Golgi region, with less than 10% present on the surface. In contrast, a similar chimera containing the transmembrane and cytoplasmic domains of the low density lipoprotein receptor (lys/LDLR) was localized to the plasma membrane, even though it endocytoses efficiently. Exchanging domains between the lys/MPR and lys/LDLR chimeras indicated that the MPR cytoplasmic domain contains the information necessary to specify the intracellular localization of the chimeric molecule. This signal must be located in the membrane-proximal third of the tail, as deletion of the last 120 residues of the 163 residue tail has no obvious effect on the distribution of lys/MPR. However, the recycling of the lys/MPR does not completely mimic that of the intact endogenous MPR, as immunofluorescence labelling shows that they are predominantly in different locations, indicating a role for the lumenal domain of the MPR in determining the steady-state distribution of the MPR itself.
- Subjects :
- Animals
Base Sequence
Cell Line
Chlorocebus aethiops
Coated Pits, Cell-Membrane metabolism
Endocytosis
Humans
Lysosomes metabolism
Molecular Sequence Data
Muramidase chemistry
Muramidase genetics
Protein Structure, Secondary
Receptor, IGF Type 2 chemistry
Receptor, IGF Type 2 genetics
Receptors, LDL chemistry
Receptors, LDL metabolism
Cell Compartmentation
Golgi Apparatus metabolism
Muramidase metabolism
Receptor, IGF Type 2 metabolism
Recombinant Fusion Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9533
- Volume :
- 107 ( Pt 4)
- Database :
- MEDLINE
- Journal :
- Journal of cell science
- Publication Type :
- Academic Journal
- Accession number :
- 8056846
- Full Text :
- https://doi.org/10.1242/jcs.107.4.923