Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail.

Canfield, William M.; Johnson, Karl; Ye, Richard D.; Gregory, Walter; Kornfeld, Stuart

doi:10.1016/s0021-9258(19)67649-0

Cited by 174 publications

(28 citation statements)

References 43 publications

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“…33,[41][42][43][44][45][46] MPR300 is also involved in endocytosis of secreted acidic hydrolases and other ligands. 19,22,47,48 Receptor endocytosis to early endosomes (EE)/sorting endosomes (SE) depends on scaffolding and cytoplasmic adaptor proteins, primarily clathrin, AP-2, epsinR and RFN126.…”

Section: Introductionmentioning

confidence: 99%

Bidirectional apical–basal traffic of the cation-independent mannose-6-phosphate receptor in brain endothelial cells

Siupka

Hersom

Lykke‐Hartmann

et al. 2017

J Cereb Blood Flow Metab

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Brain capillary endothelium mediates the exchange of nutrients between blood and brain parenchyma. This barrier function of the brain capillaries also limits passage of pharmaceuticals from blood to brain, which hinders treatment of several neurological disorders. Receptor-mediated transport has been suggested as a potential pharmaceutical delivery route across the brain endothelium, e.g. reports have shown that the transferrin receptor (TfR) facilitates transcytosis of TfR antibodies, but it is not known whether this recycling receptor itself traffics from apical to basal membrane in the process. Here, we elucidate the endosomal trafficking of the retrograde transported cation-independent mannose-6-phosphate receptor (MPR300) in primary cultures of brain endothelial cells (BECs) of porcine and bovine origin. Receptor expression and localisation of MPR300 in the endo-lysosomal system and trafficking of internalised receptor are analysed. We also demonstrate that MPR300 can undergo bidirectional apical-basal trafficking in primary BECs in co-culture with astrocytes. This is, to our knowledge, the first detailed study of retrograde transported receptor trafficking in BECs, and the study demonstrates that MPR300 can be transported from the luminal to abluminal membrane and reverse. Such trafficking of MPR300 suggests that retrograde transported receptors in general may provide a mechanism for transport of pharmaceuticals into the brain.

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Section: Introductionmentioning

confidence: 99%

Bidirectional apical–basal traffic of the cation-independent mannose-6-phosphate receptor in brain endothelial cells

Siupka

Hersom

Lykke‐Hartmann

et al. 2017

J Cereb Blood Flow Metab

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“…For instance, signals containing a casein kinase II site and a dileucine motif at the end of the cytoplasmic tail domain aid in the exit of the MPRs from the Golgi apparatus (Lobel et al, 1989;Mauxion et al, 1996). Additionally, if the receptors reach the cell surface, they can be endocytosed due to the recognition of aromatic based signals located early in the cytoplasmic tail domain (Johnson et al, 1990;Canfield et al, 1991). The cellular machinery which recognizes these signals has begun to be identified.…”

mentioning

confidence: 99%

Endosome to Golgi Retrieval of the Vacuolar Protein Sorting Receptor, Vps10p, Requires the Function of the VPS29, VPS30, and VPS35 Gene Products

Seaman

Marcusson

Cereghino

et al. 1997

The Journal of Cell Biology

377

371

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Mutations in the S. cerevisiae VPS29 and VPS30 genes lead to a selective protein sorting defect in which the vacuolar protein carboxypeptidase Y (CPY) is missorted and secreted from the cell, while other soluble vacuolar hydrolases like proteinase A (PrA) are delivered to the vacuole. This phenotype is similar to that seen in cells with mutations in the previously characterized VPS10 and VPS35 genes. Vps10p is a late Golgi transmembrane protein that acts as the sorting receptor for soluble vacuolar hydrolases like CPY and PrA, while Vps35p is a peripheral membrane protein which cofractionates with membranes enriched in Vps10p. The sequences of the VPS29, VPS30, and VPS35 genes do not yet give any clues to the functions of their products. Each is predicted to encode a hydrophilic protein with homologues in the human and C. elegans genomes. Interestingly, mutations in the VPS29, VPS30, or VPS35 genes change the subcellular distribution of the Vps10 protein, resulting in a shift of Vps10p from the Golgi to the vacuolar membrane. The route that Vps10p takes to reach the vacuole in a vps35 mutant does not depend upon Sec1p mediated arrival at the plasma membrane but does require the activity of the pre-vacuolar endosomal t-SNARE, Pep12p. A temperature conditional allele of the VPS35 gene was generated and has been found to cause missorting/secretion of CPY and also Vps10p to mislocalize to a vacuolar membrane fraction at the nonpermissive temperature. Vps35p continues to cofractionate with Vps10p in vps29 mutants, suggesting that Vps10p and Vps35p may directly interact. Together, the data indicate that the VPS29, VPS30, and VPS35 gene products are required for the normal recycling of Vps10p from the prevacuolar endosome back to the Golgi where it can initiate additional rounds of vacuolar hydrolase sorting.

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“…Other Golgi membrane proteins residing in the TGN achieve their localization through more dynamic means. TGN38, furin, and the mannose-6-phosphate receptor are localized to the TGN of mammalian cells by virtue of aromatic residue containing signals in their cytosolic tails (Bos et al, 1993;Wong and Hong, 1993;Humphrey et al, 1992;Canfield et al, 1991;Takahashi et al, 1995;Voor-hees et al, 1995;Schafer et al, 1995). These proteins are localized through a similar mechanism to that in operation at the ER: they continuously exit the TGN and are later retrieved from endosomal compartments (Kornfeld, 1992).…”

mentioning

confidence: 99%

Two Separate Signals Act Independently to Localize a Yeast Late Golgi Membrane Protein through a Combination of Retrieval and Retention

Bryant

Stevens

1997

The Journal of Cell Biology

153

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The localization of proteins to late-Golgi membranes (TGN) of Saccharomyces cerevisiae is conferred by targeting motifs containing aromatic residues in the cytosolic domains of these proteins. These signals could act by directing retrieval from a post-Golgi compartment or by preventing exit from the TGN. To investigate the mechanism of localization of yeast TGN proteins, we used the heterologous protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and luminal domains of the vacuolar protein alkaline phosphatase [ALP]), which localizes to the yeast TGN. Insertion of the aromatic residue–based TGN localization motif (FXFXD) of DPAP A into the cytosolic domain of ALP results in a protein that resides in the TGN. We demonstrate that the FXFXD motif confers Golgi localization through retrieval from a post-Golgi compartment by detecting a post-Golgi processed form of this protein in the TGN. We present an assay that uncouples retrieval-mediated Golgi localization from static retention-based localization, allowing measurement of the rate at which proteins exit the yeast TGN. We also demonstrate that the cytosolic domain of DPAP A contains additional information, separate from the retrieval motif, that slows exit from the TGN. We propose a model for DPAP A localization that involves two distinct mechanisms: one in which the FXFXD motif directs retrieval from a post-Golgi compartment, and a second that slows the rate at which DPAP A exits the TGN.

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Localization of the signal for rapid internalization of the bovine cation-independent mannose 6-phosphate/insulin-like growth factor-II receptor to amino acids 24-29 of the cytoplasmic tail.

Cited by 174 publications

References 43 publications

Bidirectional apical–basal traffic of the cation-independent mannose-6-phosphate receptor in brain endothelial cells

Bidirectional apical–basal traffic of the cation-independent mannose-6-phosphate receptor in brain endothelial cells

Endosome to Golgi Retrieval of the Vacuolar Protein Sorting Receptor, Vps10p, Requires the Function of the VPS29, VPS30, and VPS35 Gene Products

Two Separate Signals Act Independently to Localize a Yeast Late Golgi Membrane Protein through a Combination of Retrieval and Retention

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