Chapter Category: Cell Biology

From the book Protein Transport into the Endoplasmic Reticulum

Post‑Targeting Functions of Signal Peptides

Katja Kapp, Sabrina Schrempf, Marius K. Lemberg and Bernhard Dobberstein

Signal sequences are N‑terminal extensions of newly synthesized secretory and membrane proteins. They are usually 16 to 30 amino acid residues in length and comprised of a hydrophilic, usually positively charged N‑terminal region, a central hydrophobic domain and a C‑terminal region with the cleavage site for signal peptidase. Besides these common characteristics, signal sequences do not share sequence similarity and some are more than 50 amino acid residues long. In eukaryotes, signal sequences direct the insertion of proteins into the membrane of the endoplasmic reticulum and are usually cleaved off by signal peptidase. The resulting signal peptides are presumably rapidly degraded, but some still have functions on their own. Here, we describe examples of post-targeting functions of membrane‑integral signal peptides, of signal peptides released from the membrane into either the cytosol or endoplasmic reticulum lumen and of signal peptide fragments generated by intramembrane cleavage. Thus, signal peptides must be considered as an additional resource in the context of the function of secretory and membrane proteins.

Taken from the book

Protein Transport into the Endoplasmic Reticulum

Edited by: Richard Zimmermann

More chapters from the book:

Translocon Organization in Cells
Deborah E. Aronson and Erik L. Snapp

A protein’s function is a product of its inherent structural and biochemical characteristics. Equally critical to protein function are elements of its cellular environment including localization, organization and dynamics, which regulate the capacity of a protein to encounter substrates in...


Membrane Protein Biosynthesis at the Endoplasmic Reticulum
Benedict C.S. Cross and Stephen High

Current estimates suggest that 20‑30% of a typical eukaryotic genome encodes proteins that span a membrane, the majority of which are generated at the endoplasmic reticulum (ER). A remarkable proteinaceous complex embedded in the membrane of the ER, termed the ER translocon, is responsible for...


The endoplasmic reticulum (ER) is the exclusive site of secretory and integral membrane protein synthesis. The process of compartmentalizing protein synthesis to the ER occurs through a positive selection mechanism, the signal recognition particle (SRP) pathway. Growing evidence indicates the ER...


Human Pathologies of Protein Transport into the Endoplasmic Reticulum
LInda Müller, Bernd Wullich and Richard Zimmermann

Protein transport into the endoplasmic reticulum (ER) involves a protein translocase that resides in the ER membrane and is highly conserved between lower and higher eukaryotes. The Sec61 complex forms the central component of this translocase, providing a path for the newly synthesized...


Membrane Insertion of Tail-Anchored Proteins
Nica Borgese, Silvia Brambillasca, Marco Righi and Sara Colombo

Tail‑anchored (TA) proteins are a heterogeneous group of transmembrane proteins with diverse important functions that share an unusual mechanism of insertion into their target membranes. Indeed, because of the C‑terminal position of their transmembrane domain they do not have a chance to...


The Role of BiP and Its Co‑Chaperones
Johanna Dudek, Julia Benedix and Carolin Jalal

Molecular chaperones and their co-chaperones of the endoplasmic reticulum (ER) are crucial for efficient ER‑associated protein biogenesis. The major molecular chaperone of the ER, BiP, is a member of the heat shock protein 70 (Hsp70) family and cooperates with co-chaperones of the Hsp40 family,...


Structure of the Sec61-Complex
Richard Wagner, Frank Erdmann, Anke Harsman and Alf Honigmann

A conserved protein translocation channel is formed by the hetero‑trimeric Sec61 complex in eucaryotes and by SecY complex in archaea and eubacteria. Experimental observations including biochemical, biophysical and electron microscopy studies indicate that oligomers of the hetero‑trimeric...


Sec Complexes in the Yeast ER
Barrie M. Wilkinson and Colin J. Stirling

The transport of proteins across biological membranes is a process fundamental to intracellular protein trafficking and organelle biogenesis. Entry into the eukaryotic secretory pathway is initiated by the translocation of proteins across the membrane of the endoplasmic reticulum (ER). This...


Post‑Targeting Functions of Signal Peptides
Katja Kapp, Sabrina Schrempf, Marius K. Lemberg and Bernhard Dobberstein

Signal sequences are N‑terminal extensions of newly synthesized secretory and membrane proteins. They are usually 16 to 30 amino acid residues in length and comprised of a hydrophilic, usually positively charged N‑terminal region, a central hydrophobic domain and a C‑terminal region with...


Advertisements