A receptor for signal segments of secretory proteins in rough endoplasmic reticulum membranes

  title={A receptor for signal segments of secretory proteins in rough endoplasmic reticulum membranes},
  author={Siegfried Prehn and Peter J. N{\"u}rnberg and Tom A. Rapoport},
  journal={FEBS Letters},
Characterization of secretory protein translocation: ribosome-membrane interaction in endoplasmic reticulum
Control proteolysis was used to functionally inactivate rough microsomes that had previously been depleted of docking protein, and potentially two additional proteinaceous components, as yet unidentified, are involved in protein translocation.
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site- specific arrest of chain elongation that is released by microsomal membranes
It is concluded that the interaction of SRP with the amino-terminal signal peptide of the nascent chain (emerged from the large ribosomal subunit) that modulates translation and thereby causes an arrest in chain elongation.
Different modes of membrane interactions of the signal sequence of carp preproinsulin and of the insertion sequence of rabbit cytochrome b5.
The signal segment of the secretory protein carp preproinsulin is shown to be bound by a protein receptor present in the rough endoplasmic reticulum membrane, but the insertion sequence, in contrast to the signal sequence, is dissolved into the lipid bilayer of natural and artificial membranes.
Protein translocation across and integration into membranes.
  • T. Rapoport
  • Biology
    CRC critical reviews in biochemistry
  • 1986
This review concentrates mainly on the translocation of proteins across the endoplasmic reticulum membrane and cytoplasmic membrane in bacteria and the function of signal, stop-transfer, and insertion sequences will be dealt with and molecular differences discussed.
Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein
The prev i ous l y observed (Wal ter , et al . 1981 1 . Cel l Bi o l . 91 : 545 550) i nh i b i tory ef fect of SRP sel ect i vel y on the cel l f ree trans l at i on of mRNA for secretory protei n


Demonstration of specific receptors of the rough endoplasmic membrane for the signal sequence of carp preproinsulin.
The results show that stripped rough endoplasmic membranes possess specific protein-containing receptors for signal sequences on their cytoplasmic side and neither smooth endoplasmsic membranes from dog pancreas nor erythrocyte plasma membranes from rabbits are able to bind signal peptides.
A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function.
Data suggest that an initially common pathway is involved in the biogenesis of secretory proteins and at least one class of integral membrane proteins.
Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein.
Findings demonstrate that insertion of this membrane protein occurs during or immediately after protein synthesis, consistent with the concepts that the growing membrane protein is extruded across the endoplasmic reticulum membrane amino terminus first and that glycosylation is restricted to the lumenal surface of the membrane.
Nascent chicken ovalbumin contains the functional equivalent of a signal sequence
It is suggested that nascent ovalbumin contains the functional equivalent of a signal sequence for transfer across membranes, and that membrane components involved in the segregation of secretory proteins with cleaved signal sequences also function in thegregation of ovalbum in dog pancreas.
Transfer to proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
These results establish unequivocally that the information for segregation of a translation product is encoded in the mRNA itself, not in the protein- synthesizing apparatus; this provides strong evidence in support of the signal hypothesis.
Tryptic dissection and reconstitution of translocation activity for nascent presecretory proteins across microsomal membranes.
It is proposed that trypsin effects solubilization from the membrane of cytosol-exposed domain(s) involved in recognition of the signal sequence or ribosome or both, leaving behind membrane-integrated domain(S) that provide the environment for the passage of the nascent chain across the membrane.
Characterization of an endopeptidase involved in pre-protein processing.
Proteolytic removal of the pre-segment from growing nascent chains of pre-human placental lactogen (hPL) occurred during in vitro translation of placental mRNA if crude membranes derived from ascites
Inhibition of preprotein processing in ascites tumor lysates by incorporation of a leucine analog.
  • G. HortinI. Boime
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1980
These experiments demonstrate that translocation and processing of secretory proteins require structural features determined by the primary amino acid sequence.