Evidence map›Paper›PMID 33843200›Full record

ArticleACS synthetic biology2021

Optimized iLID Membrane Anchors for Local Optogenetic Protein Recruitment.

Dean E Natwick, Sean R Collins

Open access · greenAbstract read
In one paragraph

Article in ACS synthetic biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Analysis of Light-Controlled Artificial Cell-Cell Adhesions.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Shining a light on RhoA: Optical control of cell contractility.The international journal of biochemistry & cell biology · 2023
    Review
  18. Article
  19. Article
  20. Design and engineering of light-sensitive protein switches.Current opinion in structural biology · 2022
    Review
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

2 authors at 1 institution in 1 country.

Dean E NatwickDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, California 95616, United States.ORCID 0000-0003-3552-7673
Sean R CollinsDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, California 95616, United States.ORCID 0000-0002-4276-5840
University of California, Davis · US

Funding

UC Davis MCB T32 Administrative Supplement to Recognize Excellence in Diversity, Equity, Inclusion, and Accessibility (DEIA) MentorshipT32GM007377 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEDIN, FREDERIC LOUIS · 1985 to 2023
$9.9M
Rewiring Control of Leukocyte Motility for Therapeutic ApplicationDP2HD094656 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI COLLINS, SEAN RYAN · 2017 to 2017
$2.4M
Optogenetic approaches to dissect Rho GTPase signal transduction during neutrophil responses to inflammationF31HL152621 · NHLBI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI NATWICK, DEAN EDWARD · 2020 to 2020
$38k
NHLBI NIH HHS F31 HL152621NICHD NIH HHS DP2 HD094656NIGMS NIH HHS T32 GM007377
6 · The paper itself

Abstract

Optogenetic protein dimerization systems are powerful tools to investigate the biochemical networks that cells use to make decisions and coordinate their activities. These tools, including the improved Light-Inducible Dimer (iLID) system, offer the ability to selectively recruit components to subcellular locations, such as micron-scale regions of the plasma membrane. In this way, the role of individual proteins within signaling networks can be examined with high spatiotemporal resolution. Currently, consistent recruitment is limited by heterogeneous optogenetic component expression, and spatial precision is diminished by protein diffusion, especially over long time scales. Here, we address these challenges within the iLID system with alternative membrane anchoring domains and fusion configurations. Using live cell imaging and mathematical modeling, we demonstrate that the anchoring strategy affects both component expression and diffusion, which in turn impact recruitment strength, kinetics, and spatial dynamics. Compared to the commonly used C-terminal iLID fusion, fusion proteins with large N-terminal anchors show stronger local recruitment, slower diffusion of recruited components, efficient recruitment over wider gene expression ranges, and improved spatial control over signaling outputs. We also define guidelines for component expression regimes for optimal recruitment for both cell-wide and subcellular recruitment strategies. Our findings highlight key sources of imprecision within light-inducible dimer systems and provide tools that allow greater control of subcellular protein localization across diverse cell biological applications.

Indexed as

LightCell MembraneCell Surface ExtensionsGene ExpressionHEK293 CellsHumansIntracellular SpaceKineticsMembrane Fusion ProteinsModels, TheoreticalOptogeneticsPlasmidsProtein DomainsProtein MultimerizationProtein TransportSignal TransductionMembrane Fusion Proteinsmathematical modelingoptogenetics

Identifiers

PMID33843200
PMCPMC8202217
OpenAlexW3153112183

What OpenQuestion holds

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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.