Stabilization of Mutant 46-kDa Mannose 6-Phosphate Receptors by Proteasomal Inhibitor Lactacystin
نویسندگان
چکیده
منابع مشابه
Stabilization of mutant 46-kDa mannose 6-phosphate receptors by proteasomal inhibitor lactacystin.
Palmitoylation of cysteine residue 34 within the 67-amino acid cytoplasmic domain of the 46-kDa mannose 6-phosphate receptor (MPR 46), which may be anchored to the lipid bilayer, prevents the receptor from entering lysosomes (Schweizer, A., Kornfeld, S., and Rohrer, J. (1996) J. Cell Biol. 132, 577-584). In the present study, we examined the importance of the spacing between the transmembrane d...
متن کاملCloning, sequencing, and functional characterization of the murine 46-kDa mannose 6-phosphate receptor.
We have cloned and sequenced the 2175-nucleotide, full-length cDNA for the mouse 46-kDa Man 6-P receptor (46MPR) and studied its functional properties in stably transfected mouse L cells which do not express the insulin-like growth factor-II receptor/mannose 6-phosphate receptor (IGF-IIR/MPR). The 278-amino acid sequence deduced from the cDNA for the murine 46MPR shows 19 amino acid differences...
متن کاملThe carboxy-terminal peptides of 46 kDa and 300 kDa mannose 6-phosphate receptors share partial sequence homology and contain information for sorting in the early endosomal pathway.
Recycling of mannose 6-phosphate receptors was investigated by microinjection of F(ab) fragments against their carboxy-terminal peptides (residues 54-67 or 150-164 of the cytoplasmic domain of 46 kDa and 300 kDa mannose 6-phosphate receptor, respectively). For each receptor, masking the carboxy-terminal peptide by the corresponding F(ab) fragments resulted in complete depletion of the intracell...
متن کاملIdentification of mannose 6-phosphate receptors in rabbit alveolar macrophages.
Mannose 6-phosphate is an important recognition site involved in transport of newly synthesized lysosomal enzymes from the endoplasmic reticulum to lysosomes. The current study is the first demonstration of functional mannose phosphate receptors in macrophages. The receptor appears to be similar in many respects to that expressed in fibroblasts. Binding at 4 degrees C of a mannose-6-P-containin...
متن کاملRecognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein.
Tail-interacting 47-kDa protein (TIP47) binds the cytoplasmic domains of the cation-dependent (CD) and cation-independent (CI) mannose 6-phosphate receptors (MPRs) and is required for their transport from endosomes to the Golgi complex. TIP47 recognizes a phenylalanine-tryptophan signal in the CD-MPR. We show here that TIP47 interaction with the 163-residue CI-MPR cytoplasmic domain is highly c...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.50.33254