Evidence map›Paper›PMID 41362608›Full record

ArticleiScience2025

Proteomics- and BRET- screens identify SPRY2 as a Ras effector that impacts its membrane organization.

Karolina Pavic, Fiona Elizabeth Hood, Carla Jane Duval, Ganesh Babu Manoharan, Christina Laurini, Farid Ahmad Siddiqui, Stephanie Puy Lam Mo, Ian Andrew Prior, Daniel Kwaku Abankwa

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in iScience, 2025. 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

9 authors.

Karolina PavicCancer Cell Biology and Drug Discovery Group, Department of Life Sciences and Medicine, University of Luxembourg, 4362 Esch-sur-Alzette, Luxembourg.
Fiona Elizabeth HoodDepartment of Molecular and Clinical Cancer Medicine, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 3BX, UK.
Carla Jane DuvalCancer Cell Biology and Drug Discovery Group, Department of Life Sciences and Medicine, University of Luxembourg, 4362 Esch-sur-Alzette, Luxembourg.
Ganesh Babu ManoharanCancer Cell Biology and Drug Discovery Group, Department of Life Sciences and Medicine, University of Luxembourg, 4362 Esch-sur-Alzette, Luxembourg.
Christina LauriniCancer Cell Biology and Drug Discovery Group, Department of Life Sciences and Medicine, University of Luxembourg, 4362 Esch-sur-Alzette, Luxembourg.
Farid Ahmad SiddiquiInstitute of Biomedicine, University of Turku, 20520 Turku, Finland.
Stephanie Puy Lam MoDepartment of Molecular and Clinical Cancer Medicine, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 3BX, UK.
Ian Andrew PriorDepartment of Molecular and Clinical Cancer Medicine, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool L69 3BX, UK.
Daniel Kwaku AbankwaCancer Cell Biology and Drug Discovery Group, Department of Life Sciences and Medicine, University of Luxembourg, 4362 Esch-sur-Alzette, Luxembourg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Few regulators of K-Ras plasma membrane organization are known. We combined TurboID-based proximity proteomics with a BRET screen to identify eight potential K-Ras G-domain interactors. We focused on APLP2, which indirectly engages with C-Raf in immediate proximity to K-Ras, and SPRY2, which exhibits properties of an effector. Co-immunoprecipitation and BRET assays revealed that the SPRY2 C-terminal half binds oncogenic RasG12V more than full-length SPRY2. Both forms localize to the plasma membrane, but this localization and binding to K-Ras are disrupted by inhibitors of K-Ras membrane anchorage or activity. Mutations at the predicted interface of K-Ras and SPRY2's C-terminal region affect the interaction. Both full-length SPRY2 and its C-terminal fragment promote the differentiation of C2C12 muscle cells, a process requiring MAPK pathway inhibition. Finally, SPRY2 homo- and hetero-oligomerizes with SPRY4. We propose that active K-Ras recruits SPRY2 dimers to the membrane, where they block Ras effector access.

Indexed as

Membrane architectureMolecular biologyProteomics

Identifiers

PMID41362608
PMCPMC12682140

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.