Evidence map›Paper›PMID 42758831›Full record

ArticleScience advances2026

GTPase cycle and ER membrane regulate cargo handover during cotranslational protein targeting.

Ruilin Qian, Radoslaw J Gora, SangYoon Chung, Jae Ho Lee, Sowmya Chandrasekar, Max Feng-Yu Wang, Shimon Weiss, Shu-Ou Shan

Abstract read
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In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Ruilin QianDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0009-0001-7138-5556
Radoslaw J GoraDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0000-0002-3677-066X
SangYoon ChungDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Jae Ho LeeDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0000-0002-8663-3209
Sowmya ChandrasekarDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
Max Feng-Yu WangDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0009-0009-1713-4287
Shimon WeissDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.ORCID 0000-0002-0720-5426
Shu-Ou ShanDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.ORCID 0000-0002-6526-1733

Funding

Supplement: Accurate Molecular Decision Making during Protein BiogenesisR35GM136321 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Shu-ou Shan · 2020 to 2026
$6.7M
NIGMS NIH HHS R35 GM136321
6 · The paper itself

Abstract

Signal recognition particle (SRP), a universally conserved protein-targeting machine, cotranslationally recognizes signal sequences of nascent endomembrane proteins and engages the SRP receptor (SR) at the endoplasmic reticulum (ER) membrane to unload the translating ribosome. The mechanism of membrane-associated steps in this pathway remains unclear. Here, we address this question using pre-steady-state and single-molecule fluorescence measurements. SR induces release of the signal sequence from SRP and detachment of the SRP guanosine triphosphatase (GTPase) domain from the ribosome. Despite the dissolution of these contacts, SR acts as a tether to stabilize SRP association with the ribosome. Guanosine 5'-triphosphate (GTP) hydrolysis in the SRP-SR complex abolishes this stabilizing effect to facilitate ribosome-nascent chain complex (RNC) release from SRP. The ER membrane selectively promotes a prehandover conformation of the RNC-SRP-SR complex, in which delayed GTP hydrolysis optimizes the transition from targeting to translocation. Our findings provide a high-resolution model for key steps during cargo handover at the ER and highlight the critical role of fine-tuned GTPase activity in the SRP pathway.

Indexed as

Endoplasmic ReticulumGTP PhosphohydrolasesIntracellular MembranesProtein BiosynthesisSignal Recognition ParticleGuanosine TriphosphateHydrolysisProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideRibosomesGTP PhosphohydrolasesGuanosine TriphosphateReceptors, Cytoplasmic and NuclearReceptors, Peptidesignal peptide receptorSignal Recognition Particle

Identifiers

PMID42758831
PMCPMC13588191

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.