Evidence map›Paper›PMID 22157745›Full record

ArticleThe EMBO journal2012

A palmitoylation switch mechanism regulates Rac1 function and membrane organization.

Inmaculada Navarro-Lérida, Sara Sánchez-Perales, María Calvo, Carles Rentero, Yi Zheng, Carlos Enrich, Miguel A Del Pozo

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
6.9field-weighted citation impact, top 2% of its field
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

107 citing papers in PubMed, 176 citations in OpenAlex.

  1. Review
  2. Article
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  4. How Functional Variants Reconfigure the Rac2 Conformational Landscape.bioRxiv : the preprint server for biology · 2026
    Article
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  7. Article
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  12. The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
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  19. Review
  20. Article

47 more citing papers are in PubMed but not listed here.

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

7 authors at 5 institutions in 2 countries.

Inmaculada Navarro-LéridaDepartment of Vascular Biology, Integrin Signaling Laboratory, Centro Nacional de Investigaciones Cardiovasculares, Madrid, Spain.
Sara Sánchez-Perales
María Calvo
Carles Rentero
Yi Zheng
Carlos Enrich
Miguel A Del Pozo
Centro Nacional de Biotecnología · ESUniversitat de Barcelona · ESCincinnati Children's Hospital Medical Center · USConsorci Institut D'Investigacions Biomediques August Pi I Sunyer · ESSpanish National Centre for Cardiovascular Research · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small GTPase Rac1 plays important roles in many processes, including cytoskeletal reorganization, cell migration, cell-cycle progression and gene expression. The initiation of Rac1 signalling requires at least two mechanisms: GTP loading via the guanosine triphosphate (GTP)/guanosine diphosphate (GDP) cycle, and targeting to cholesterol-rich liquid-ordered plasma membrane microdomains. Little is known about the molecular mechanisms governing this specific compartmentalization. We show that Rac1 can incorporate palmitate at cysteine 178 and that this post-translational modification targets Rac1 for stabilization at actin cytoskeleton-linked ordered membrane regions. Palmitoylation of Rac1 requires its prior prenylation and the intact C-terminal polybasic region and is regulated by the triproline-rich motif. Non-palmitoylated Rac1 shows decreased GTP loading and lower association with detergent-resistant (liquid-ordered) membranes (DRMs). Cells expressing no Rac1 or a palmitoylation-deficient mutant have an increased content of disordered membrane domains, and markers of ordered membranes isolated from Rac1-deficient cells do not correctly partition in DRMs. Importantly, cells lacking Rac1 palmitoylation show spreading and migration defects. These data identify palmitoylation as a mechanism for Rac1 function in actin cytoskeleton remodelling by controlling its membrane partitioning, which in turn regulates membrane organization.

Indexed as

Amino Acid SequenceBiopolymersCell MembraneGuanosine TriphosphateMolecular Sequence DataPalmitic AcidProtein Prenylationrac1 GTP-Binding ProteinSequence Homology, Amino AcidBiopolymersGuanosine TriphosphatePalmitic Acidrac1 GTP-Binding Protein

Identifiers

PMID22157745
PMCPMC3273400
OpenAlexW2105083581

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.