Secretory protein translocation across membranes—the role of the ‘docking protein’

Meyer, David I.; Krause, E.; Dobberstein, Bernhard

doi:10.1038/297647a0

Cited by 638 publications

(350 citation statements)

References 22 publications

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“…Such translocation is mediated by a hydrophobic signal sequence, a signal recognition protein (SRP), and an SRP receptor (docking protein) located in the ER. [11][12][13] Secretory proteins are then packaged into vesicles in the Golgi apparatus and exit cells via membrane fusion, 14 a process that can be partially suppressed by microtubule inhibitors. 15 Re-entry into the cells is mostly accomplished by receptor-dependent endocytosis, although other mechanisms have been reported.…”

Section: Discussionmentioning

confidence: 99%

Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells

Fang

Koch

et al. 1998

Gene Ther

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Herpes simplex virus type 1 (HSV-1) VP22 was recently fused proteins were localized to the nuclei of transfected reported to mediate intercellular trafficking of a protein cells. Quantitative analysis of GFP-positive cells, however, fused to the C-terminus of VP22. To explore the application showed no significant increase in intercellular protein trafof such trafficking, we constructed plasmids expressing ficking for cells transfected with either fusion protein comgreen fluorescent protein (GFP) fused to the C-terminus of pared with a lacZ-expressing plasmid. Our results suggest either wild-type VP22 or a 160 amino acid peptide from that the use of HSV-1 VP22 for mediating intercellular VP22. In vitro studies showed that the majority of both trafficking of transgene products is limited.

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Section: Discussionmentioning

confidence: 99%

Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells

Fang

Koch

et al. 1998

Gene Ther

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“…In eukaryotes, translation is arrested or retarded until the ribosome-nascent chain complex is situated at the translocon. [34][35][36][37][38] …”

Section: The Srp-dependent Targeting Cycle In Eukaryotes and Prokaryotesmentioning

confidence: 99%

Use of synthetic signal sequences to explore the protein export machinery

Clérico¹,

Maki²,

Gierasch³

2008

Biopolymers

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The information for correct localization of newly synthesized proteins in both prokaryotes and eukaryotes resides in self‐contained, often transportable targeting sequences. Of these, signal sequences specify that a protein should be secreted from a cell or incorporated into the cytoplasmic membrane. A central puzzle is presented by the lack of primary structural homology among signal sequences, although they share common features in their sequences. Synthetic signal peptides have enabled a wide range of studies of how these “zipcodes” for protein secretion are decoded and used to target proteins to the protein machinery that facilitates their translocation across and integration into membranes. We review research on how the information in signal sequences enables their passenger proteins to be correctly and efficiently localized. Synthetic signal peptides have made possible binding and crosslinking studies to explore how selectivity is achieved in recognition by the signal sequence‐binding receptors, signal recognition particle, or SRP, which functions in all organisms, and SecA, which functions in prokaryotes and some organelles of prokaryotic origins. While progress has been made, the absence of atomic resolution structures for complexes of signal peptides and their receptors has definitely left many questions to be answered in the future. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 307–319, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…Certain peptides can act as signals to localize proteins to particular organelles such as the ER, the mitochondria (Verner and Schatz, 1988) and the nucleus (Silver and Hall, 1988). Several proteins have been identified that mediate the recognition of ER-destined proteins and their subsequent translocation across or assembly into the ER membrane (Walter and Blobel, 1980;Meyer et al, 1982;Tajima et al, 1986; Wiedrnan et al, 1987). Receptors have been proposed for mitochondrial signal peptides (Pfaller and Neupert, 1987;Pfanner et al, 1987) and recently a receptor for protein import into chloroplasts has been identified (Pain et al, 1988).…”

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confidence: 99%

A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.

Sadler

Chiang

Kurihara

et al. 1989

The Journal of Cell Biology

289

184

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Abstract. When nuclear localization sequences (termed NLS) are placed at the N terminus of cytochrome ca, a mitochondrial inner membrane protein, the resulting hybrid proteins do not assemble into mitochondria when synthesized in the yeast Saccharomyces cerevisiae. Cells lacking mitochondrial cytochrome c~, but expressing the hybrid NLScytochrome c, proteins, are unable to grow on glycerol since the hybrid proteins are associated primarily with the nucleus. A similar hybrid protein with a mutant NLS is transported to and assembled into the mitochondria. To identify proteins that might be involved in recognition of nuclear localization signals, we isolated conditional-lethal mutants (npl, for nuclear protein localization) that missorted NLS-cytochrome c, to the mitochondria, allowing growth on glycerol. The gene corresponding to one complementation group (NPLI) encodes a protein with homology to DnaJ, an Escherichia coli heat shock protein, npU-1 is allelic to sec63, a gene that affects transit of nascent secretory proteins across the endoplasmic reticulum. Rothblatt, J. A., R. J. Deshaies, S. L. Sanders, G. Daum, and R. Schekman. 1989. J. Cell Biol. 109:2641-2652. The npU mutants reported here also weakly affect translocation of preprocarboxypeptidaseY across the ER membrane. A normally nuclear hybrid protein containing a NLS fused to invertase and a nucleolar protein are not localized to the nucleus in np11/sec63 cells at the nonpermissive temperature. Thus, NPLI/SEC63 may act at a very early common step in localization of proteins to the nucleus and the ER. Alternatively, by affecting ER and nuclear envelope assembly, npll may indirectly alter assembly of proteins into the nucleus.ACH organelle in a eukaryotic cell has a distinct set of proteins that are necessary for its specific function. Certain peptides can act as signals to localize proteins to particular organelles such as the ER, the mitochondria (Verner and Schatz, 1988) and the nucleus (Silver and Hall, 1988). Several proteins have been identified that mediate the recognition of ER-destined proteins and their subsequent translocation across or assembly into the ER membrane (Walter and Blobel, 1980;Meyer et al., 1982;Tajima et al., 1986; Wiedrnan et al., 1987). Receptors have been proposed for mitochondrial signal peptides (Pfaller and Neupert, 1987;Pfanner et al., 1987) and recently a receptor for protein import into chloroplasts has been identified (Pain et al., 1988). By analogy, similar components may exist for localization of proteins to the nucleus.Nuclear localization sequences (NLS)' are stretches of amino acids that are capable of redirecting nonnuclear pro-1. Abbreviations used in this paper: DAPI, diamidinophenylindole; EMS, ethyl methanesulfonate; NLS, nuclear localization sequences; preproCPY, preprocarboxypeptidase Y.teins such as/$-galactosidase to the nucleus. When the first 74 amino acids of the yeast DNA binding protein GAL4 are joined to/~-galactosidase, the result is a fusion protein that is found exclusively in the yeast nucleus as...

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Secretory protein translocation across membranes—the role of the ‘docking protein’

Cited by 638 publications

References 22 publications

Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells

Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells

Use of synthetic signal sequences to explore the protein export machinery

A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.

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