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Science 25 July 1997: Vol. 277. no. 5325, pp. 556 - 558 DOI: 10.1126/science.277.5325.556
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Reports
A Di-Acidic Signal Required for Selective Export from the Endoplasmic Reticulum
Noriyuki Nishimura,
William E. Balch
*
Transport of membrane proteins between intracellular compartments
requires specific sequences in the protein cytoplasmic domain to direct
packaging into vesicle shuttles. A sequence that mediates export from
the endoplasmic reticulum (ER) has proved elusive. A di-acidic signal
(Asp-X-Glu, where X represents any amino acid) on the cytoplasmic tail
of vesicular stomatitis virus glycoprotein (VSV-G) and other
cargo molecules was required for efficient recruitment to vesicles
mediating export from the ER in baby hamster kidney cells. The
existence of such a signal provides evidence that export from the ER
occurs through a selective mechanism.
Departments of Molecular and Cell Biology, The Scripps Research
Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
*
To whom correspondence should be addressed. E-Mail:
webalch{at}scripps.edu
Read the Full Text
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- Golgi Network Targeting and Plasma Membrane Internalization Signals in Vaccinia Virus B5R Envelope Protein.
- B. M. Ward and B. Moss (2000)
J. Virol.
74, 3771-3780
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- Sec24p and Iss1p Function Interchangeably in Transport Vesicle Formation from the Endoplasmic Reticulum in Saccharomyces cerevisiae.
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Mol. Biol. Cell
11, 983-998
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- Identification and Characterization of a Novel Golgi Protein, Golgin-67.
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275, 4137-4144
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- Identification of CD7 as a Cognate of the Human K12 (SECTM1) Protein.
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275, 3431-3437
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- Molecular and Conformational Features of a Transport-Relevant Domain in the C-Terminal Tail of the Vasopressin V2 Receptor.
- G. Krause, R. Hermosilla, A. Oksche, C. Rutz, W. Rosenthal, and R. Schülein (2000)
Mol. Pharmacol.
57, 232-242
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- Lumenal targeted GFP, used as a marker of soluble cargo, visualises rapid ERGIC to Golgi traffic by a tubulo-vesicular network.
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J. Cell Sci.
113, 3151-3159
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- Talin controls the exit of the integrin alpha 5 beta 1 from an early compartment of the secretory pathway.
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J. Cell Sci.
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- ERGIC-53 and traffic in the secretory pathway.
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J. Cell Sci.
113, 587-596
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- Efficient Export of the Vesicular Stomatitis Virus G Protein from the Endoplasmic Reticulum Requires a Signal in the Cytoplasmic Tail That Includes Both Tyrosine-based and Di-acidic Motifs.
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Mol. Biol. Cell
11, 13-22
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- Mannose-dependent Endoplasmic Reticulum (ER)-Golgi Intermediate Compartment-53-mediated ER to Golgi Trafficking of Coagulation Factors V and VIII.
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274, 32539-32542
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- Saturation of the Endoplasmic Reticulum Retention Machinery Reveals Anterograde Bulk Flow.
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PLANT CELL
11, 2233-2248
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- A Di-acidic (DXE) Code Directs Concentration of Cargo during Export from the Endoplasmic Reticulum.
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- Protein Targeting to Endoplasmic Reticulum by Dilysine Signals Involves Direct Retention in Addition to Retrieval.
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274, 15080-15084
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- The Transmembrane Domain of Hepatitis C Virus Glycoprotein E1 Is a Signal for Static Retention in the Endoplasmic Reticulum.
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- Mutation of the YXXL Endocytosis Motif in the Cytoplasmic Tail of Pseudorabies Virus gE.
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- The Endoplasmic Reticulum—Gateway of the Secretory Pathway.
- A. Vitale and J. Denecke (1999)
PLANT CELL
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- Identification of Domains Mediating Transcriptional Activation and Cytoplasmic Export in the Caudal Homeobox Protein Cdx-3.
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