The DOI matches its Crossref record.
Enhanced Degradation of EGF Receptors by a Sorting Nexin, SNX1
Abstract
The vectorial movement of proteins requires specific recognition by components of the vesicular trafficking machinery. A protein, sorting nexin-1 (SNX1), was identified in a human cell line that bound to a region of the epidermal growth factor receptor (EGFR) containing the lysosomal targeting code. SNX1 contains a region of homology to a yeast vacuolar sorting protein, and overexpression of SNX1 decreased the amount of EGFR on the cell surface as a result of enhanced rates of constitutive and ligand-induced degradation. Thus, SNX1 is likely to play a role in sorting EGFR to lysosomes.
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SNX1 directs the EGFR to the lysosome, accelerating its degradation and thus downregulating the growth factor signal transmitted by EGFR.
“This is in sharp contrast to SNX1 which directs the EGFR to the lysosome, accelerating its degradation and thus downregulating the growth factor signal transmitted by EGFR (Kurten et al ., 1996).”
From The PX‐domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor (2002) · cites this paper as Kurten et al., 1996
Certain sorting nexins (SNXs) are involved in receptor sorting and/or membrane trafficking.
“Prompted by recent findings that certain SNXs are involved in receptor sorting and/or membrane trafficking (Kurten et al ., 1996; Parks et al ., 2001; Xu et al ., 2001), we investigated whether the interaction of SNX17 with members of the LDLR family plays a role in the endocytic pathway of these receptors, and used the well characterized LDLR pathway for these studies.”
From The PX‐domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor (2002) · cites this paper as Kurten et al., 1996
Several members of the sorting nexin family have been shown to interact with transmembrane receptors involved in cell signaling, in some cases via their carboxyl-terminal domain and in others via the PX domain.
“Several members of the sorting nexin family have been shown to interact with transmembrane receptors involved in cell signaling (8), in some cases via their carboxyl-terminal domain (23) and in others, via the PX domain (28).”
From Sorting Motifs in the Intracellular Domain of the Low Density Lipoprotein Receptor Interact with a Novel Domain of Sorting Nexin-17 (2004) · cites this paper as [23]
Human SNX1 was first identified by its ability to interact with the lysosomal targeting signal of the epidermal growth factor (EGF) receptor.
“Human SNX1 was first identified by its ability to interact with the lysosomal targeting signal of the epidermal growth factor (EGF) receptor (23).”
From Sorting Motifs in the Intracellular Domain of the Low Density Lipoprotein Receptor Interact with a Novel Domain of Sorting Nexin-17 (2004) · cites this paper as [23]
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Research works printed but not linked: 10
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- AUSUBEL F.M., CURRENT PROTOCOLS MO (1995).
- CADENA D.L., THE INTRACELLULAR TYROSINE KINASE DOMAIN OF THE EPIDERMAL GROWTH-FACTOR RECEPTOR UNDERGOES A CONFORMATIONAL CHANGE UPON AUTOPHOSPHORYLATION, JOURNAL OF BIOLOGICAL CHEMISTRY 269, 260 (1994). · DOI
- EKENA K, THE SACCHAROMYCES-CEREVISIAE MVP1 GENE INTERACTS WITH VPS1 AND IS REQUIRED FOR VACUOLAR PROTEIN SORTING, MOLECULAR AND CELLULAR BIOLOGY 15, 1671 (1995). · DOI
- FRENCH A.R., POSTENDOCYTIC TRAFFICKING OF EPIDERMAL GROWTH FACTOR-RECEPTOR COMPLEXES IS MEDIATED THROUGH SATURABLE AND SPECIFIC ENDOSOMAL INTERACTIONS, JOURNAL OF BIOLOGICAL CHEMISTRY 269, 15749 (1994). · DOI
- JOHNSON K.F., THE CYTOPLASMIC TAIL OF THE MANNOSE 6-PHOSPHATE INSULIN-LIKE GROWTH FACTOR-II RECEPTOR HAS 2 SIGNALS FOR LYSOSOMAL-ENZYME SORTING IN THE GOLGI, JOURNAL OF CELL BIOLOGY 119, 249 (1992). · DOI
- LETOURNEUR F, A NOVEL DI-LEUCINE MOTIF AND A TYROSINE-BASED MOTIF INDEPENDENTLY MEDIATE LYSOSOMAL TARGETING AND ENDOCYTOSIS OF CD3 CHAINS, CELL 69, 1143 (1992). · DOI · Paper page
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- 10.1016/0092-8674(93)90662-A · DOI
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The emerging role of sorting nexins in cardiovascular diseases
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Metadata
- Authors
- Kurten, R. C., Cadena, D. L., & Gill, G. N.
- Venue
- Science
- Published
- 1996-05-17
- Volume
- 272
- Issue
- 5264
- Pages
- 1008-1010
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 322
- References
- 0
- Language
- en
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