SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites

Lakkaraju, Asvin K.K.; Mary, Camille; Scherrer, Anne; Johnson, Arthur E.; Strub, Katharina

doi:10.1016/j.cell.2008.02.049

Cited by 136RNA and protein synthesis mechanismsEndoplasmic Reticulum Stress and DiseaseCellular transport and secretion

SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites

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Lakkaraju, Asvin K.K., Mary, Camille, Scherrer, Anne, Johnson, Arthur E., Strub, Katharina·2008·Cell

DOI 10.1016/j.cell.2008.02.049PMC PMC2430734

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Abstract

SRP is essential for targeting nascent chains to the endoplasmic reticulum, and it delays nascent chain elongation in cell-free translation systems. However, the significance of this function has remained unclear. We show that efficient protein translocation into the ER is incompatible with normal cellular translation rates due to rate-limiting concentrations of SRP receptor (SR). We complemented mammalian cells depleted of SRP14 by expressing mutant versions of the protein lacking the elongation arrest function. The absence of a delay caused inefficient targeting of preproteins leading to defects in secretion, depletion of proteins in the endogenous membranes, and reduced cell growth. The detrimental effects were reversed by either reducing the cellular protein synthesis rate or increasing SR expression. SRP therefore ensures that nascent chains remain translocation competent during the targeting time window dictated by SR. Since SRP-signal sequence affinities vary, the delay may also regulate which proteins are preferentially targeted.

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SRP14 enhanced productivity of recombinant IgG in CHO cells when overexpressed.
“Likewise, signal recognition particle 14 (SRP14), which targets secreted proteins to the endoplasmic reticulum membrane, enhanced productivity of recombinant IgG in CHO cells when overexpressed (Lakkaraju et al., 2008;Le Fourn et al., 2014).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Lakkaraju et al., 2008
The section ‘Elongation arrest-defective SRP impairs the accumulation of membrane and secreted proteins’ (page unavailable) shows that functional SRP14 is important for secretion: restoring it in depleted 293T cells restored normal SEAP secretion. The paper does not report SRP14 overexpression increasing recombinant IgG productivity in CHO cells; searches for CHO cells, IgG, and overexpression found no such result. (LLM, conf=0.87)
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Authors: Lakkaraju, A. K. K., Mary, C., Scherrer, A., Johnson, A. E., & Strub, K.
Affiliations: University of Geneva (CH)
Texas A&M Health Science Center (US)
Corresponding author: Strub, Katharina
ORCID: Lakkaraju, Asvin K.K.
Mary, Camille
Venue: Cell
Publisher: Elsevier BV
Published: 2008-05
Volume: 133
Issue: 3
Pages: 440-451
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2008.02.049
PMC: PMC2430734
OpenAlex: W2043436209
Cited by: 136
References: 45
Citations by year: 2026: 9 · 2025: 2 · 2024: 7 · 2023: 7 · 2022: 5 · 2021: 20 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 4 · 2015: 9 · 2014: 12 · 2013: 6 · 2012: 7
FWCI: 5.08
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1903 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Archive ouverte UNIGE (University of Geneva) (acceptedVersion, other-oa)
Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
Funders: Welch Foundation
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
National Institutes of Health
National Institute of General Medical Sciences (R01 GM 26494, R01GM026494)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: signal recognition particle, SRP receptor, protein translocation, endoplasmic reticulum targeting, translation rate, protein secretion, cell growth
MeSH terms: Amino Acid Sequence, Animals, Cell Cycle, Cell Line, Cell-Free System, HeLa Cells, Humans, Molecular Sequence Data, Peptide Chain Elongation, Translational, Protein Synthesis Inhibitors, Signal Recognition Particle, Endoplasmic Reticulum, Rough, Protein Transport, Green Fluorescent Proteins

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SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites

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