Evidence map›Paper›PMID 19458198›Full record

ArticleMolecular biology of the cell2009

Clathrin functions in the absence of the terminal domain binding site for adaptor-associated clathrin-box motifs.

John R Collette, Richard J Chi, Douglas R Boettner, Isabel M Fernandez-Golbano, Rachael Plemel, Alex J Merz, Maria Isabel Geli, Linton M Traub, Sandra K Lemmon

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Weak Molecular Interactions in Clathrin-Mediated Endocytosis.Frontiers in molecular biosciences · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Getting in touch with the clathrin terminal domain.Traffic (Copenhagen, Denmark) · 2012
    Review
  18. Article
  19. 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

9 authors at 4 institutions in 2 countries.

John R ColletteDepartment of Molecular and Cellular Pharmacology, University of Miami, Miami, FL 33101, USA.
Richard J Chi
Douglas R Boettner
Isabel M Fernandez-Golbano
Rachael Plemel
Alex J Merz
Maria Isabel Geli
Linton M Traub
Sandra K Lemmon
University of Miami · USInstitut de Biologia Molecular de Barcelona · ESUniversity of Washington · USUniversity of Pittsburgh · US

Funding

Dynamics of Endomembrane Docking and FusionR01GM077349 · NIGMS · UNIVERSITY OF WASHINGTON · PI MERZ, ALEXEY JARRELL · 2006 to 2024
$6.1M
SUPPRESSORS OF CLATHRIN DEFICIENCY IN YEASTR01GM055796 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LEMMON, SANDRA K. · 1998 to 2015
$4.7M
TRAINING PROGRAMS IN CARDIOVASCULAR PHARMACOLOGYT32HL007188 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SZCZESNA-CORDARY, DANUTA · 1985 to 2011
$3.8M
CLATHRIN COATED VESICLES AND LYSOSOME FUNCTIONR01DK053249 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TRAUB, LINTON M. · 1998 to 2011
$3.0M
Regulation of endoytosis by clathrin light chain.F32GM084677 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BOETTNER, DOUGLAS ROBB · 2008 to 2010
$149k
NHLBI NIH HHS T32 HL007188NHLBI NIH HHS T32-HL07188NIDDK NIH HHS DK-53249NIDDK NIH HHS R01 DK053249NIGMS NIH HHS F32 GM084677NIGMS NIH HHS F32-GM084677NIGMS NIH HHS GM-084677NIGMS NIH HHS R01 GM055796NIGMS NIH HHS R01 GM077349
6 · The paper itself

Abstract

Clathrin is involved in vesicle formation in the trans-Golgi network (TGN)/endosomal system and during endocytosis. Clathrin recruitment to membranes is mediated by the clathrin heavy chain (HC) N-terminal domain (TD), which forms a seven-bladed beta-propeller. TD binds membrane-associated adaptors, which have short peptide motifs, either the clathrin-box (CBM) and/or the W-box; however, the importance of the TD binding sites for these motifs has not been tested in vivo. We investigated the importance of the TD in clathrin function by generating 1) mutations in the yeast HC gene (CHC1) to disrupt the binding sites for the CBM and W-box (chc1-box), and 2) four TD-specific temperature-sensitive alleles of CHC1. We found that TD is important for the retention of resident TGN enzymes and endocytosis of alpha-factor; however, the known adaptor binding sites are not necessary, because chc1-box caused little to no effect on trafficking pathways involving clathrin. The Chc1-box TD was able to interact with the endocytic adaptor Ent2 in a CBM-dependent manner, and HCs encoded by chc1-box formed clathrin-coated vesicles. These data suggest that additional or alternative binding sites exist on the TD propeller to help facilitate the recruitment of clathrin to sites of vesicle formation.

Indexed as

Adaptor Proteins, Vesicular TransportAllelesAmino Acid MotifsAmino Acid SequenceAminopeptidasesBinding SitesChitin SynthaseClathrinClathrin-Coated VesiclesClathrin Heavy ChainsEndocytosisGreen Fluorescent ProteinsMolecular Sequence DataMutationProtein BindingProtein Processing, Post-TranslationalAdaptor Proteins, Vesicular TransportAminopeptidasesAPE1 protein, S cerevisiaeCHC1 protein, S cerevisiaeChitin SynthaseClathrinClathrin Heavy ChainsGreen Fluorescent ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19458198
PMCPMC2710826
OpenAlexW2122588131

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.