Evidence map›Paper›PMID 9891074›Full record

ArticleMolecular and cellular biology1999

Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis.

M Achiriloaie, B Barylko, J P Albanesi

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 172 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022
    Article
  6. Impact of CaBiomolecules · 2022
    Article
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  11. Review
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  13. Review
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  15. CaThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

5 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

3 authors at 1 institution in 1 country.

M AchiriloaieDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
B Barylko
J P Albanesi
The University of Texas Southwestern Medical Center · US

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
REGULATION OF DYNAMIN I IN SYNAPTIC TRANSMISSIONR01GM055562 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI ALBANESI, JOSEPH P · 1998 to 2001
$557k
NIGMS NIH HHS 2-T32 GM07062-22NIGMS NIH HHS GM55562-01A2NIGMS NIH HHS R01 GM055562NIGMS NIH HHS T32 GM007062
6 · The paper itself

Abstract

Pleckstrin homology (PH) domains are found in numerous membrane-associated proteins and have been implicated in the mediation of protein-protein and protein-phospholipid interactions. Dynamin, a GTPase required for clathrin-dependent endocytosis, contains a PH domain which binds to phosphoinositides and participates in the interaction between dynamin and the betagamma subunits of heterotrimeric G proteins. The PH domain is essential for expression of phosphoinositide-stimulated GTPase activity of dynamin in vitro, but its involvement in the endocytic process is unknown. We expressed a series of dynamin PH domain mutants in cultured cells and determined their effect on transferrin uptake by those cells. Endocytosis is blocked in cells expressing a PH domain deletion mutant and a point mutant that fails to interact with phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. In contrast, expression of a point mutant with unimpaired PI(4,5)P2 interaction has no effect on transferrin uptake. These results demonstrate the significance of the PH domain for dynamin function and suggest that its role may be to mediate interactions between dynamin and phosphoinositides.

Indexed as

PhosphoproteinsAnimalsBinding SitesBlood ProteinsCOS CellsDynaminsEndocytosisGene ExpressionGTP PhosphohydrolasesMutationPhosphatidylinositol 4,5-DiphosphateRatsRecombinant ProteinsTransfectionTransferrinBlood ProteinsDynaminsGTP PhosphohydrolasesPhosphatidylinositol 4,5-DiphosphatePhosphoproteinsplatelet protein P47Recombinant ProteinsTransferrin

Identifiers

PMID9891074
PMCPMC116069
OpenAlexW2149897005

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.