Evidence map›Paper›PMID 25419208›Full record

ArticleAdvanced functional materials2014

Flipping the Switch on Clathrin-Mediated Endocytosis using Thermally Responsive Protein Microdomains.

Martha K Pastuszka, Curtis T Okamoto, Sarah F Hamm-Alvarez, J Andrew MacKay

Abstract read
In one paragraph

Article in Advanced functional materials, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Elastin-like polypeptide switches: A design strategy to detect multimeric proteins.Protein science : a publication of the Protein Society · 2017
    Article
  14. Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines.Journal of controlled release : official journal of the Controlled Release Society · 2016
    Review
  15. Review
  16. Engineering structure and function using thermoresponsive biopolymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology
    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

4 authors at 1 institution in 1 country.

Martha K PastuszkaDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California. 1985 Zonal Avenue, Los Angeles 90033-9121.
Curtis T OkamotoDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California. 1985 Zonal Avenue, Los Angeles 90033-9121.
Sarah F Hamm-AlvarezDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California. 1985 Zonal Avenue, Los Angeles 90033-9121.
J Andrew MacKayDepartment of Pharmacology and Pharmaceutical Sciences, University of Southern California. 1985 Zonal Avenue, Los Angeles 90033-9121.
University of Southern California · US

Funding

USC/NORRIS COMPREHENSIVE CANCER CENTER (CORE) SUPPORTP30CA014089 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Fumito Ito · 1985 to 2026
$181.4M
Research Supplements to Promote DiversityR01EY011386 · NEI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI HAMM-ALVAREZ, SARAH F · 1996 to 2025
$9.3M
A rapid, reversible switch for controlling intracellular traffickingR21EB012281 · NIBIB · UNIVERSITY OF SOUTHERN CALIFORNIA · PI MACKAY, JOHN ANDREW · 2010 to 2011
$438k
NCI NIH HHS P30 CA014089NEI NIH HHS R01 EY011386NIBIB NIH HHS R21 EB012281
6 · The paper itself

Abstract

A ubiquitous approach to study protein function is to knock down activity (gene deletions, siRNA, small molecule inhibitors, etc) and study the cellular effects. Using a new methodology, this manuscript describes how to rapidly and specifically switch off cellular pathways using thermally responsive protein polymers. A small increase in temperature stimulates cytosolic elastin-like polypeptides (ELPs) to assemble microdomains. We hypothesize that ELPs fused to a key effector in a target macromolecular complex will sequester the complex within these microdomains, which will bring the pathway to a halt. To test this hypothesis, we fused ELPs to clathrin-light chain (CLC), a protein associated with clathrin-mediated endocytosis. Prior to thermal stimulation, the ELP fusion is soluble and clathrin-mediated endocytosis remains 'on.' Increasing the temperature induces the assembly of ELP fusion proteins into organelle-sized microdomains that switches clathrin-mediated endocytosis 'off.' These microdomains can be thermally activated and inactivated within minutes, are reversible, do not require exogenous chemical stimulation, and are specific for components trafficked within the clathrin-mediated endocytosis pathway. This temperature-triggered cell switch system represents a new platform for the temporal manipulation of trafficking mechanisms in normal and disease cell models and has applications for manipulating other intracellular pathways.

Indexed as

clathrin-light chainclathrin-mediated endocytosiselastin-like polypeptideinverse phase transition temperatureSynthetic biology

Identifiers

PMID25419208
PMCPMC4235962
OpenAlexW2123920190

What OpenQuestion holds

Textmetadata
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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.