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1
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0016785996
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Intracellular Aspects of the Processing of Protein Synthesis
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(1975)
Science
, vol.189
, pp. 347-358
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Palade1
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2
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0026555196
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Molecular Dissection of the Secretory Pathway
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(1992)
Nature
, vol.355
, pp. 409-415
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Rothman1
Orci2
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4
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0025764613
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Recycling of Proteins Between the Endoplasmic Reticulum and Golgi Complex
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(1991)
Curr Opin Cell Biol
, vol.3
, pp. 585-591
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Pelham1
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5
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0025184422
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Identification of a Consensus Motif for Retention of Transmembrane Proteins in the Endoplasmic Reticulum
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(1990)
EMBO J
, vol.9
, pp. 3153-3162
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Jackson1
Nilsson2
Peterson3
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7
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0022975133
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The Trans Golgi Network: Sorting at the Exit Site of the Golgi Complex
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(1986)
Science
, vol.234
, pp. 438-443
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Griffiths1
Simons2
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9
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0022385726
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Compartmental Organization of the Golgi Stack
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(1885)
Cell
, vol.42
, pp. 13-21
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Dunphy1
Rothman2
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10
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0026503134
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The Golgi Complex: In Vitro Veritas?
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of special interest, A thorough review of current knowledge of the Golgi complex with some provocative new ideas.
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(1992)
Cell
, vol.68
, pp. 829-840
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Mellman1
Simons2
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11
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0026934508
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Pathways of Protein Sorting and Membrane Traffic Between the Rough Endoplasmic Reticulum and the Golgi Complex
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of special interest, An interesting review that focuses on membrane traffic at the ER-Golgi interface. A model of transport through the Golgi by ‘cistemal progression’ is presented.
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(1992)
Semin Cell Biol
, vol.3
, pp. 343-355
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Saraste1
Kuismanen2
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12
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0027472941
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Overlapping Distribution of Two Glycosylttansferases in the Golgi Apparatus of HeLa Cells
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of special interest, This is the first co-localization of two different glycosyltransferases at the electron microscope level. Endogenous GT and transfected GnTl showed substantial overlap in the transcistema of HeLa cells, although neighboring cistemae on either side contained mostly one or the other transferase. Unique mixtures of transferases were suggested to create unique cistemae.
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(1993)
J Cell Biol
, vol.120
, pp. 5-13
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Nilsson1
Pypaekt2
Hoe3
Slusarewicz4
Berger5
Warren6
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13
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0024431691
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Glycosyltransferases. Structure, Localization, and Control of Cell Type-Specific Glycosylation
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(1989)
J Biol Chem
, vol.264
, pp. 17615-17618
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Paulson1
Colley2
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14
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0026325913
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Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans
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(1991)
The Journal of Cell Biology
, vol.115
, pp. 1521-1534
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Moreman1
Robbins2
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16
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0024315732
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Translocation of Nucleotide Sugars and Nucleotide Sulfate Across Membranes of the Endoplasmic Reticulum and the Golgi Apparatus
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(1989)
Biochem Soc Trans
, vol.17
, pp. 447-448
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Milla1
Capasso2
Hirschberg3
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18
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0025733702
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Mammalian Subtilisins: The Long-Sought Dibasic Processing Endoproteases
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(1991)
Cell
, vol.66
, pp. 1-3
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Barb1
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22
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0023580390
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A Specific Transmembrane Domain of a Coronavirus El Glycoprotein is Required for its Retention in the Golgi Region
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(1987)
J Cell Biol
, vol.105
, pp. 1205-1214
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Machamer1
Rose2
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23
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0025940737
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A Golgi Retention Signal in a Membrane Spanning Domain of Coronavirus El Protein
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of special interst, The first Golgi localization signal to be described was found in the first of three TMDs from Coronavirus M (E1) protein. This TMD was sufficient for retention of two reporters (VSV G protein and the α-subunit of human chorionic gonadotropin) in early Golgi membranes, and several mutations in the TMD disrupted retention (resulting in transport to the plasma membrane).
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(1991)
J Cell Biol
, vol.115
, pp. 19-30
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Swift1
Machamer2
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27
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0009698725
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Enzymes Associated with Glycosylalion
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of special interest, A concise review of reports describing targeting signals of three glycosyltransferases. Careful attention is given to the chimeras generated, the cell lines used and the results obtained in each study.
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(1992)
Curr Opin Struct Blol
, vol.2
, pp. 701-709
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Shaper1
Shaper2
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28
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0026072695
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The Membrane Spanning Domain of β-1,4-Galactosyltmnsfemse Specifies Trans Golgi Localization
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of special interest, Using the human invariant chain as the reporter, the lumenal half of the GT TMD was demonstrated to be sufficient for trans-Golgi localization. A cytoplasmic sequence (from GT or the invariant chain) was required for efficient retention.
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(1991)
EMBO J
, vol.10
, pp. 1367-1375
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Nilsson1
Lucocq2
Mackay3
Warren4
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29
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0026607683
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Golgi Retention of a Trans-Golgi Membrane Protein, Galactosyltransfetase, Requires Cysteine and Histidine Residues Within the Membrane-Anchoring Domain
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of special interest, Cysteine and histidine residues from the GT TMD were shown to be important for Golgi localization in the transferrin receptor TMD background. The lumenal domain reporter was the a-subunit of human chorionic gonadotropin.
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(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 4319-4323
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Aoki1
Lee2
Yamaguchi3
Dubois4
Fukuda5
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30
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0026793378
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2-Terminal Fragment That Includes the Cytoplasmic and Transmembrane Domain is Sufficient for Golgi Retention
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of special interest, The amino-terminal domain (cytoplasmic tail and TMD) of GT was sufficient for Golgi targeting of pyruvate kinase. Constructs with either the long or short tail (from the two GT isoforms) were both targeted to the trans-Golgi as detected by immunoelectron microscopy.
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(1992)
J Biol Chem
, vol.267
, pp. 9241-9247
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Russo1
Shaper2
Taatjes3
Shaper4
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31
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0026784536
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The Signal for Golgi Retention of Bovine β1,2-GALatosyltransferase is in the Transmembrane Domain
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of special interest, The amino terminus of GT directed Golgi localization of ovalbumin. Most of the cytoplasmic tail could be deleted, suggesting that the GT TMD contained the Golgi-targeting signal.
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(1992)
J Biol Chem
, vol.267
, pp. 4084-4096
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Teasdale1
D'Agostaro2
Gleeson3
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32
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0025990802
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Sequences Within and Adjacent to the Transmembrane Segment of α-2,6-Sialyltransfemse Specify Golgi Retention
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of special interest, The ST TMD retained a bipartite reporter (dipeptidyl peptidase N/ lysozyme) in the Golgi. The most efficient retention required flanking sequences. The TMD could be replaced with poly-Leu and the protein was still retained in the Golgi, suggesting targeting information also existed in the ST flanking sequences.
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(1991)
EMBO J
, vol.10
, pp. 3577-3588
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Munro1
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33
-
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0026738935
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The Signal Anchor and Stem Regions of the β-Galactoside α2,6-Sialyltransferase May Each Act to Localize the Enzyme to the Golgi Apparatus
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of special interest, Soluble ST lacking the cytoplasmic tail and TMD (but with the stem) was retained in the Golgi, but the stem was not required for retention of membrane-bound ST. In addition, replacing the ST TMD with that from a plasma membrane protein still gave Golgi localization, suggesting that both TMD and stem contained targeting information.
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(1992)
J Biol Chem
, vol.267
, pp. 7784-7793
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Colley1
Lee2
Paulson3
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34
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0026598516
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The 17-Residue Transmembrane Domain of β-Galactoside α2,6-SialylaAnsferase is Sufficient for Golgi Retention
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of special interest, The TMD of ST (without the stem region) was sufficient for Golgi localization of dipeptidyl peptidase N as reporter. No cell surface molecules were detected by pulse-chase analysis, suggesting that the ST TMD was acting as a retention signal.
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(1992)
J Cell Biol
, vol.117
, pp. 245-258
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Wong1
Low2
Hong3
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35
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0026686809
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The Transmembrane Domain of N-Glucosaminyltmnsferase I Contains a Golgi Retention Signal
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of special interest, The TMD of GnTI was sufficient for Golgi localization of dipeptidyl peptidase N, although flanking sequences increased the efficiency of retention.
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(1992)
J Biol Chem
, vol.267
, pp. 10122-10126
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Tang1
Wong2
Low3
Hong4
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36
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0026459645
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The Transmembrane and Flanking Sequences of β1,2-NAcetylglucosaminyltransferase I Specify Medial Golgi Localization
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of special interest, The TMD and short cytoplasmic tail of GnTl retained ovalbumin in medial-Golgi cistemae as determined by immunoelectron microscopy.
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(1992)
J Biol Chem
, vol.267
, pp. 24433-24440
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Burke1
Petttit2
Schachter3
Sarkar4
Gleeson5
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37
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0025942525
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Evidence for a Molecular Distinction between Golgi and Cell Surface Forms of β1,4-Galactosyltransferase
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(1991)
J Biol Chem
, vol.266
, pp. 15984-15991
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Lopez1
Youakim2
Evans3
Shur4
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38
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0027157541
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Characterization of Two cis-Regulatory Regions in the Murine β1,4-Galactosyltransferase Gene: Evidence for a Negative Regulatory Ele ment that Controls Initiation at the Proximal Site
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(1993)
J Biol Chem
, vol.268
, pp. 14348-14349
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Harduin-lepers1
Shaaper2
Shaper3
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40
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0027395956
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Localization of the TGN38 to the Trans Golgi Network: Involvement of a Cytoplasmic Tyrosine-containing Sequence
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of special interest, A tyrosine-containing signal in the TGN38 cytoplasmic tail was required for TGN localization of the Tac reporter. One mutation within this tyrosine signal prevented TGN localization without blocking internalization from the plasma membrane, suggesting that discrete determinants in the signal mediate these two events.
-
(1993)
J Cell Biol
, vol.120
, pp. 1123-1135
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Humphrey1
Peters2
Yuan3
Bonifacino4
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42
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0025789665
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Lysosomal Membrane Glycoproteins
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(1991)
J Biol Chem
, vol.266
, pp. 21327-21330
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Fukuda1
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43
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0027080272
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Mutation of a Tyrosine Localization Signal in the Cytosolic Tail of Yeast Kex2 Protease Disrupts Golgi Retention and Re sults in Default Transport to the Vacuole
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of special interest, A Tyr-containing signal in the cytoplasmic tail of Kex2p was required for Golgi retention. A mutation in this sequence as well as overexpression of wild-type Kex2p resulted in transport to the vacuole, suggesting that this may be the default destination for membrane proteins in yeast.
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(1992)
Mol Biol Cell
, vol.3
, pp. 1353-1371
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Wilcox1
Redding2
Wright3
Fuller4
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44
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0027085824
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Yeast Kexlp Is a Golgi-Associated Membrane Protein: Deletions in a Cytoplasmic Targeting Domain Result in Mislocalization to the Vacuolar Membrane
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of special interest, Golgi retention of Kex1p required its cytoplamic tail, as several truncations of this sequence resulted in delivery to the vacuole.
-
(1992)
J Cell Biol
, vol.119
, pp. 1459-1468
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Cooper1
Bussey2
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45
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0026727566
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Membrane Protein Sorting in the Yeast Secretory Pathway: Evidence That the Vacuole May Be the Default Compartment
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of special interest, The signal for localization of DPAP A to the Golgi was contained within a 22 amino acid region of the cytoplasmic tail that has five phenylalanine residues (one of which may function like a tyrosine-containing signal). As above, loss of retention in the Golgi resulted in transport to the vacuole.
-
(1992)
J Cell Biol
, vol.119
, pp. 69-83
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Roberts1
Nothwehr2
Stevens3
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46
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0026742306
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Selective and Immediate Effects of Clathrin Heavy Chain Mutations on Golgi Membrane Protein Retention in Saccharomyces cerevesiae
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⊎] suggest that tyrosine motifs in cytoplasmic tails of TGN residents interact directly or indirectly with clathrin for efficient retention.
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(1992)
J Cell Biol
, vol.118
, pp. 531-540
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Seeger1
Payne2
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48
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0023375833
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Two Integral Membrane Proteins Located in the Cis-Middle and Trams-Part of the Golgi System Acquire Sialylated N-Linked Carbohydrates and Display Different Turnovers and Sensitivity to cAMP-Dependent Phosphorylation
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(1987)
J Cell Biol
, vol.105
, pp. 215-227
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Yuan1
Barriocanal2
Bonifacino3
Sandoval4
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