Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum

Letourneur, François; Gaynor, Erin C.; Hennecke, Silke; Démollière, Corinne; Duden, Rainer; Emr, Scott D.; Riezman, Howard; Cosson, Pierre

doi:10.1016/0092-8674(94)90011-6

Cited by 760 publications

(718 citation statements)

References 39 publications

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“…These results are not easy to interpret, because COPI is implicated in intra-Golgi traffic, and as shown above, Golgi function is required for GFP-Snc1p recycling. However, cop1-1 cells show little defect in secretion or endocytosis to the vacuole even at 37°C, and at 25°C sec21-1 cells are also fully secretion competent (Letourneur et al, 1994;Hicke et al, 1997). We cannot therefore exclude the possibility that COPI is the coat responsible for mediating the retrieval of GFP-Snc1p from endosomes.…”

Section: Retrieval Of Snc1p From Early Endosomesmentioning

confidence: 74%

Specific Retrieval of the Exocytic SNARE Snc1p from Early Yeast Endosomes

Lewis

Nichols

Prescianotto-Baschong

et al. 2000

MBoC

Self Cite

333

515

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Many endocytosed proteins in yeast travel to the vacuole, but some are recycled to the plasma membrane. We have investigated the recycling of chimeras containing green fluorescent protein (GFP) and the exocytic SNARE Snc1p. GFP-Snc1p moves from the cell surface to internal structures when Golgi function or exocytosis is blocked, suggesting continuous recycling via the Golgi. Internalization is mediated by a conserved cytoplasmic signal, whereas diversion from the vacuolar pathway requires sequences within and adjacent to the transmembrane domain. Delivery from the Golgi to the surface is also influenced by the transmembrane domain, but the requirements are much less specific. Recycling requires the syntaxins Tlg1p and Tlg2p but not Pep12p or proteins such as Vps4p and Vps5p that have been implicated in late endosome–Golgi traffic. Subtle changes to the recycling signal cause GFP-Snc1p to accumulate preferentially in punctate internal structures, although it continues to recycle to the surface. The internal GFP-Snc1p colocalizes with Tlg1p, and immunofluorescence and immunoelectron microscopy reveal structures that contain Tlg1p, Tlg2p, and Kex2p but lack Pep12p and Sec7p. We propose that these represent early endosomes in which sorting of Snc1p and late Golgi proteins occurs, and that transport can occur directly from them to the Golgi apparatus.

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Section: Retrieval Of Snc1p From Early Endosomesmentioning

confidence: 74%

Specific Retrieval of the Exocytic SNARE Snc1p from Early Yeast Endosomes

Lewis

Nichols

Prescianotto-Baschong

et al. 2000

MBoC

Self Cite

333

515

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“…To test the hypothesis that this localization is mechanistically involved in the F12 phenotype, a KKXX sorting motif (lysine, lysine, methionine, and proline [KKMP]) was inserted at the C terminus of a CD8.NefNL4-3 hybrid protein (CD8.NefKKXX). KKXX motifs bind the ␤ subunit of the COP-I coatomer and mediate the retrieval of cargo from later compartments back to the ER during biosynthetic transport (7,26). We analyzed whether the addition of the KKXX motif to Nef induced a subcellular localization similar to that of the CD8.NefF12 chimera in NIH 3T3 cells by using confocal microscopy.…”

Section: Resultsmentioning

confidence: 99%

Nef Binds p6* in GagPol during Replication of Human Immunodeficiency Virus Type 1

Costa

Zheng

Sabotič

et al. 2004

J Virol

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Human immunodeficiency virus type 1 (HIV-1), the causative agent of AIDS, encodes 16 distinct proteins that are expressed differentially during the viral replicative cycle. Initially, the early regulatory proteins Tat and Rev and the socalled negative effector (Nef) are translated from multiply spliced mRNA species. During late phases, singly spliced or unspliced transcripts direct the expression of viral accessory proteins (viral proteins R and U [Vpr and Vpu] and viral infectivity factor [Vif]), as well as structural group-specific antigen (Gag), Gag and polymerase (GagPol), and envelope (Env) polyproteins (see reference 20 and references therein).

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“…According to their paper, however, the rerl mutation does not seem to affect the recycling of this protein. More recently, Cosson and Letourneur showed in collaboration with Emr's group and Riezman that components of coatomer or COP I (Retlp, Sec2lp, and Sec27p) are involved in the retrieval of KKXX proteins (Letourneur et al, 1994). It is possible that the retrieval of Secl2p also utilizes this COP I system.…”

Section: Rer1mentioning

confidence: 99%

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

Sato

Nishikawa

Nakano

1995

MBoC

101

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Yeast Sec12p, a type II transmembrane glycoprotein, is required for formation of transport vesicles from the endoplasmic reticulum (ER). Biochemical and morphological analyses have suggested that Sec12p is localized to the ER by two mechanisms: static retention in the ER and dynamic retrieval from the early region of the Golgi apparatus. The rer1 mutant we isolated in a previous study mislocalizes the authentic Sec12p to the later compartments of the Golgi. To understand the role of RER1 on Sec12p localization, we cloned the gene and determined its reading frame. RER1 encodes a hydrophobic protein of 188 amino acid residues containing four putative membrane spanning domains. The rer1 null mutant is viable. Even in the rer1 disrupted cells, immunofluorescence of Sec12p stains the ER, implying that the retention system is still operating in the mutant. To determine the subcellular localization of Rer1p, an epitope derived from the influenza hemagglutinin was added to the C-terminus of Rer1p and the cells expressing this tagged but functional protein were observed by immunofluorescence microscopy. The anti-HA monoclonal antibody stains the cells in a punctate pattern that is typical for Golgi proteins and clearly distinct from the ER staining. This punctate staining was in fact exaggerated in the sec7 mutant that accumulates the Golgi membranes at the restrictive temperature. Furthermore, double staining of Rer1p and Ypt1p, a GTPase that is known to reside in the Golgi apparatus, showed good colocalization. Subcellular fractionation experiments indicated that the fractionation pattern of Rer1p was similar to that of an early Golgi protein, Och1p. From these results, we suggest that Rer1p functions in the Golgi membrane to return Sec12p that has escaped from the static retention system of the ER.

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Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum

Cited by 760 publications

References 39 publications

Specific Retrieval of the Exocytic SNARE Snc1p from Early Yeast Endosomes

Specific Retrieval of the Exocytic SNARE Snc1p from Early Yeast Endosomes

Nef Binds p6* in GagPol during Replication of Human Immunodeficiency Virus Type 1

Membrane protein retrieval from the Golgi apparatus to the endoplasmic reticulum (ER): characterization of the RER1 gene product as a component involved in ER localization of Sec12p.

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