The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum

Looking at the variety of the thousands of different polypeptides that have been focused on in the research on the endoplasmic reticulum from the last five decades taught us one humble lesson: no one size fits all. Cells use an impressive array of components to enable the safe transport of protein c...

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Bibliographic Details
Published in:International journal of molecular sciences 2021-12, Vol.23 (1), p.143
Main Authors: Tirincsi, Andrea, Sicking, Mark, Hadzibeganovic, Drazena, Haßdenteufel, Sarah, Lang, Sven
Format: Article
Language:English
Subjects:
Animals
Biodiversity
C-Terminus
Cell size
Cytosol - metabolism
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
GET
Humans
Hydrophobicity
Hypotheses
Membrane proteins
Plasma
Polypeptides
Protein Sorting Signals - physiology
protein targeting
Protein transport
Protein Transport - physiology
Proteins
Proteins - metabolism
Review
Ribosomes
Signal recognition particle
Signal Recognition Particle - metabolism
SND
SRP
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Summary:Looking at the variety of the thousands of different polypeptides that have been focused on in the research on the endoplasmic reticulum from the last five decades taught us one humble lesson: no one size fits all. Cells use an impressive array of components to enable the safe transport of protein cargo from the cytosolic ribosomes to the endoplasmic reticulum. Safety during the transit is warranted by the interplay of cytosolic chaperones, membrane receptors, and protein translocases that together form functional networks and serve as protein targeting and translocation routes. While two targeting routes to the endoplasmic reticulum, SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins), prefer targeting determinants at the N- and C-terminus of the cargo polypeptide, respectively, the recently discovered SND (SRP-independent) route seems to preferentially cater for cargos with non-generic targeting signals that are less hydrophobic or more distant from the termini. With an emphasis on targeting routes and protein translocases, we will discuss those functional networks that drive efficient protein topogenesis and shed light on their redundant and dynamic nature in health and disease.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms23010143