Evidence map›Paper›PMID 15456883›Full record

ArticleMolecular and cellular biology2004

Phosphatidylinositol-4,5-bisphosphate-rich plasma membrane patches organize active zones of endocytosis and ruffling in cultured adipocytes.

Shaohui Huang, Larry Lifshitz, Varsha Patki-Kamath, Richard Tuft, Kevin Fogarty, Michael P Czech

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 79 citations in OpenAlex.

  1. Small Nucleolar RNA fromNon-coding RNA · 2025
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Rab38 targets to lamellar bodies and normalizes their sizes in lung alveolar type II epithelial cells.American journal of physiology. Lung cellular and molecular physiology · 2011
    Article
  14. Article
  15. Article
  16. Novel role of cPLA(2)alpha in membrane and actin dynamics.Cellular and molecular life sciences : CMLS · 2010
    Article
  17. Article
  18. Article
  19. Article
  20. Kinetics of the interaction of myo1c with phosphoinositides.The Journal of biological chemistry · 2009
    Article
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

6 authors at 2 institutions in 2 countries.

Shaohui HuangProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation St., Worcester, MA 01605, USA.
Larry Lifshitz
Varsha Patki-Kamath
Richard Tuft
Kevin Fogarty
Michael P Czech
Institute of Molecular Medicine · INUniversity of Massachusetts Chan Medical School · US

Funding

SUBCELLULAR LOCALIZATION OF PI 3-KINASE SIGNALINGP01DK060564 · NIDDK · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI FOGARTY, KEVIN EDWARD · 2001 to 2011
$13.9M
NIDDK NIH HHS DK60564NIDDK NIH HHS P01 DK060564
6 · The paper itself

Abstract

A major regulator of endocytosis and cortical F-actin is thought to be phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2] present in plasma membranes. Here we report that in 3T3-L1 adipocytes, clathrin-coated membrane retrieval and dense concentrations of polymerized actin occur in restricted zones of high endocytic activity. Ultrafast-acquisition and superresolution deconvolution microscopy of cultured adipocytes expressing an enhanced green fluorescent protein- or enhanced cyan fluorescent protein (ECFP)-tagged phospholipase Cdelta1 (PLCdelta1) pleckstrin homology (PH) domain reveals that these zones spatially coincide with large-scale PtdIns(4,5)P2-rich plasma membrane patches (PRMPs). PRMPs exhibit lateral dimensions exceeding several micrometers, are relatively stationary, and display extensive local membrane folding that concentrates PtdIns(4,5)P2 in three-dimensional space. In addition, a higher concentration of PtdIns(4,5)P2 in the membranes of PRMPs than in other regions of the plasma membrane can be detected by quantitative fluorescence microscopy. Vesicular structures containing both clathrin heavy chains and PtdIns(4,5)P2 are revealed immediately beneath PRMPs, as is dense F actin. Blockade of PtdIns(4,5)P2 function in PRMPs by high expression of the ECFP-tagged PLCdelta1 PH domain inhibits transferrin endocytosis and reduces the abundance of cortical F-actin. Membrane ruffles induced by the expression of unconventional myosin 1c were also found to localize at PRMPs. These results are consistent with the hypothesis that PRMPs organize active PtdIns(4,5)P2 signaling zones in the adipocyte plasma membrane that in turn control regulators of endocytosis, actin dynamics, and membrane ruffling.

Indexed as

3T3 CellsActinsAdipocytesAnimalsCell MembraneCell Membrane StructuresCells, CulturedClathrinClathrin-Coated VesiclesCytoskeletonEndocytosisFluorescent DyesIsoenzymesMiceMicroscopy, FluorescenceModels, BiologicalActinsClathrinFluorescent DyesIsoenzymesMyo1c protein, mouseMyosinsMyosin Type IPhosphatidylinositol 4,5-DiphosphatePhospholipase C deltaPlcd1 protein, mouseRecombinant Fusion ProteinsTransferrinType C Phospholipases

Identifiers

PMID15456883
PMCPMC517906
OpenAlexW2096964838

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.