Römisch, Karin, Miller, Frederick W, Dobberstein, Bernhard, High, Stephen
Abstract The 54 kDa subunit of the signal recognition particle (SRP54) binds to the signal sequences of nascent secretory and membrane proteins and it contributes to the targeting of these precursors...
An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY (1994)
Luirink Joen, Van Der Weijden, Coen C., Oudega, Bauke, High, Stephen, ...
In Escherichia coli, a signal recognition particle (SRP) has been identified which binds specifically to the signal sequence of presecretory proteins and which appears to be essential for efficient...
High, Stephen, Andersen, Soren S. L., Görlich, Dirk, Hartmann, Enno, Prehn, Siegfried, Rapoport, Tom A., ...
We have identified membrane components which are adjacent to type I and type II signal-anchor proteins during their insertion into the membrane of the ER. Using two different cross-linking approaches...
High, Stephen, Martoglio, Bruno, Görlich, Dirk, Andersen, Soren S. L., Ashford, Anthony J., Giner, Angelika, ...
A chemically charged amber suppressor tRNA was used to introduce the photoactivatable amino acid (Tmd)Phe at a selected position within the signal sequence of the secretory protein preprolactin. This...
Lütcke, Henrich, High, Stephen, Römisch, Karin, Ashford, Anthony J., Dobberstein, Bernhard
The signal recognition particle (SRP) binds to signal sequences when they emerge from a translating ribosome and targets the complex of ribosome, nascent chain and SRP to the membrane of the rough...
High, Stephen, Görlich, Dirk, Wiedmann, Martin, Rapoport, Tom A., Dobberstein, Bernhard
Using a photocross-linking approach we have investigated the cytosolic and membrane components involved in the targeting and insertion of signalanchor proteins into the membrane of the ER. The...
Requirements for the Membrane Insertion of Signal-anchor Type Proteins (1991)
High, Stephen, Flint, Nicholas, Dobberstein, Bernhard
Proteins which are inserted and anchored in the membrane of the ER by an uncleaved signalanchor sequence can assume two final orientations. Type I signal-anchor proteins translocate the NH2 terminus...
High, Stephen, Dobberstein, Bernhard
The signal sequence of nascent preprolactin interacts with the 54-kD protein of the signal recognition particle (SRP54). To identify the domain or site on SRP54 that interacts with the signal...
Swanton, Eileithyia, Sheehan, John, Bishop, Naomi, High, Stephen, Woodman, Philip
Specificity of vesicular transport is determined by pair-wise interaction between receptors (SNAP receptors or SNAREs) associated with a transport vesicle and its target membrane. Two additional...
Oliver, Jason D., Roderick, H. Llewelyn, Llewellyn, David H., High, Stephen
ERp57 is a lumenal protein of the endoplasmic reticulum (ER) and a member of the protein disulfide isomerase (PDI) family. In contrast to archetypal PDI, ERp57 interacts specifically with newly...
Meacock, Suzanna L., Lecomte, Fabienne J.L., Crawshaw, Samuel G., High, Stephen
We have been studying the insertion of the seven transmembrane domain (TM) protein opsin to gain insights into how the multiple TMs of polytopic proteins are integrated at the endoplasmic reticulum...
Role of calnexin in the glycan-independent quality control of proteolipid protein
Swanton, Eileithyia, High, Stephen, Woodman, Philip
The endoplasmic (ER) quality control apparatus ensures that misfolded or unassembled proteins are not deployed within the cell, but are retained in the ER and degraded. A glycoprotein-specific system...
Signal recognition particle mediates post-translational targeting in eukaryotes
Abell, Benjamin M, Pool, Martin R, Schlenker, Oliver, Sinning, Irmgard, High, Stephen
Signal recognition particle (SRP) plays a central role in the delivery of classical secretory and membrane proteins to the endoplasmic reticulum (ER). All nascent chains studied to date dissociate...
Swanton, Eileithyia, Holland, Andrew, High, Stephen, Woodman, Philip
Pelizaeus–Merzbacher disease (PMD) is a dysmyelinating disease caused by mutations, deletions, or duplications of the proteolipid protein (PLP) gene. Mutant forms of PLP are retained in the...
A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
Crawshaw, Samuel G., Martoglio, Bruno, Meacock, Suzanna L., High, Stephen
The endoplasmic reticulum (ER) exerts a quality control over newly synthesized proteins and a variety of components have been implicated in the specific recognition of aberrant or misfolded...
Di Jeso, Bruno, Park, Young-nam, Ulianich, Luca, Treglia, A. Sonia, Urbanas, Malene L., High, Stephen, ...
We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with...
Römisch, Karin, Miller, Frederick W, Dobberstein, Bernhard, High, Stephen
The 54 kDa subunit of the signal recognition particle (SRP54) binds to the signal sequences of nascent secretory and membrane proteins and it contributes to the targeting of these precursors to the...
Swanton, Eileithyia, Sheehan, John, Bishop, Naomi, High, Stephen, Woodman, Philip
Specificity of vesicular transport is determined by pair-wise interaction between receptors (SNAP receptors or SNAREs) associated with a transport vesicle and its target membrane. Two additional...
Oliver, Jason D., Roderick, H. Llewelyn, Llewellyn, David H., High, Stephen
ERp57 is a lumenal protein of the endoplasmic reticulum (ER) and a member of the protein disulfide isomerase (PDI) family. In contrast to archetypal PDI, ERp57 interacts specifically with newly...
Meacock, Suzanna L., Lecomte, Fabienne J.L., Crawshaw, Samuel G., High, Stephen
We have been studying the insertion of the seven transmembrane domain (TM) protein opsin to gain insights into how the multiple TMs of polytopic proteins are integrated at the endoplasmic reticulum...
Role of calnexin in the glycan-independent quality control of proteolipid protein
Swanton, Eileithyia, High, Stephen, Woodman, Philip
The endoplasmic (ER) quality control apparatus ensures that misfolded or unassembled proteins are not deployed within the cell, but are retained in the ER and degraded. A glycoprotein-specific system...
Signal recognition particle mediates post-translational targeting in eukaryotes
Abell, Benjamin M, Pool, Martin R, Schlenker, Oliver, Sinning, Irmgard, High, Stephen
Signal recognition particle (SRP) plays a central role in the delivery of classical secretory and membrane proteins to the endoplasmic reticulum (ER). All nascent chains studied to date dissociate...
Swanton, Eileithyia, Holland, Andrew, High, Stephen, Woodman, Philip
Pelizaeus–Merzbacher disease (PMD) is a dysmyelinating disease caused by mutations, deletions, or duplications of the proteolipid protein (PLP) gene. Mutant forms of PLP are retained in the...
A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase
Crawshaw, Samuel G., Martoglio, Bruno, Meacock, Suzanna L., High, Stephen
The endoplasmic reticulum (ER) exerts a quality control over newly synthesized proteins and a variety of components have been implicated in the specific recognition of aberrant or misfolded...
Di Jeso, Bruno, Park, Young-nam, Ulianich, Luca, Treglia, A. Sonia, Urbanas, Malene L., High, Stephen, ...
We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with...
Römisch, Karin, Miller, Frederick W, Dobberstein, Bernhard, High, Stephen
The 54 kDa subunit of the signal recognition particle (SRP54) binds to the signal sequences of nascent secretory and membrane proteins and it contributes to the targeting of these precursors to the...
Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum
Callan, Anna C., Bunning, Sandra, Jones, Owen T., High, Stephen, Swanton, Eileithyia
TorsinA is a widely expressed AAA+ (ATPases associated with various cellular activities) ATPase of unknown function. Previous studies have described torsinA as a type II protein with a cleavable...
Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core
Wilson, Cornelia M., Roebuck, Quentin, High, Stephen
Protein N-glycosylation is widespread among biological systems, and the fundamental process of transferring a lipid-linked glycan to suitable asparagine residues of newly synthesized proteins occurs...
Rabu, Catherine, Wipf, Peter, Brodsky, Jeffrey L., High, Stephen
Tail-anchored (TA) protein synthesis at the endoplasmic reticulum (ER) represents a distinct and novel process that provides a paradigm for understanding post-translational membrane insertion in...