Evidence map›Paper›PMID 11694597›Full record

ArticleMolecular biology of the cell2001

In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation.

H A Watson, M J Cope, A C Groen, D G Drubin, B Wendland

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Candida albicansmSphere · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Molecular basis for coupling the plasma membrane to the actin cytoskeleton during clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Functions of actin in endocytosis.Cellular and molecular life sciences : CMLS · 2009
    Review
  20. 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

5 authors at 2 institutions in 1 country.

H A WatsonDepartment of Biology, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
M J Cope
A C Groen
D G Drubin
B Wendland
University of California, Berkeley · USJohns Hopkins University · US

Funding

The budding yeast endocytic pathwayR01GM050399 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 1997 to 2015
$5.9M
MOLECULAR ANALYSIS OF ENDOCYTOSIS PROTEINS IN YEASTR01GM060979 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WENDLAND, BEVERLY R · 2000 to 2013
$4.3M
NIGMS NIH HHS GM50399NIGMS NIH HHS GM60979NIGMS NIH HHS R01 GM050399NIGMS NIH HHS R01 GM060979
6 · The paper itself

Abstract

The yeast actin-regulating kinases Ark1p and Prk1p are signaling proteins localized to cortical actin patches, which may be sites of endocytosis. Interactions between the endocytic proteins Pan1p and End3p may be regulated by Prk1p-dependent threonine phosphorylation of Pan1p within the consensus sequence [L/I]xxQxTG. We identified two Prk1p phosphorylation sites within the Pan1p-binding protein Ent1p, a yeast epsin homologue, and demonstrate Prk1p-dependent phosphorylation of both threonines. Converting both threonines to either glutamate or alanine mimics constitutively phosphorylated or dephosphorylated Ent1p, respectively. Synthetic growth defects were observed in a pan1-20 ENT1(EE) double mutant, suggesting that Ent1p phosphorylation negatively regulates the formation/activity of a Pan1p-Ent1p complex. Interestingly, pan1-20 ent2 Delta but not pan1-20 ent1 Delta double mutants had improved growth and endocytosis over the pan1-20 mutant. We found that actin-regulating Ser/Thr kinase (ARK) mutants exhibit endocytic defects and that overexpressing either wild-type or alanine-substituted Ent1p partially suppressed phenotypes associated with loss of ARK kinases, including growth, endocytosis, and actin localization defects. Consistent with synthetic growth defects of pan1-20 ENT1(EE) cells, overexpressing glutamate-substituted Ent1p was deleterious to ARK mutants. Surprisingly, overexpressing the related Ent2p protein could not suppress ARK kinase mutant phenotypes. These results suggest that Ent1p and Ent2p are not completely redundant and may perform opposing functions in endocytosis. These data support the model that, as for clathrin-dependent recycling of synaptic vesicles, yeast endocytic protein phosphorylation inhibits endocytic functions.

Indexed as

Adaptor Proteins, Signal TransducingFungal ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsActinsAdaptor Proteins, Vesicular TransportBinding SitesCarrier ProteinsConsensus SequenceCytoskeletonEndocytosisGreen Fluorescent ProteinsLuminescent ProteinsNeuropeptidesPhosphorylationProtein Kinase CActinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCarrier ProteinsENT1 protein, S cerevisiaeENT2 protein, S cerevisiaeepsinFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsNeuropeptidesPRK1 protein, S cerevisiaeProtein Kinase Cprotein kinase NProtein Serine-Threonine KinasesReceptor Protein-Tyrosine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSorbitolThreonineVesicular Transport Proteins

Identifiers

PMID11694597
PMCPMC60284
OpenAlexW2128609040

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.