Evidence map›Paper›PMID 25631817›Full record

ArticleMolecular biology of the cell2015

Pan1 regulates transitions between stages of clathrin-mediated endocytosis.

Mary Katherine Bradford, Karen Whitworth, Beverly Wendland

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  11. Mechanisms of clathrin-mediated endocytosis.Nature reviews. Molecular cell biology · 2018
    Review
  12. A Global Analysis of Kinase Function inFrontiers in cellular and infection microbiology · 2018
    Article
  13. Article
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  15. Article
  16. Review
  17. 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

3 authors at 1 institution in 1 country.

Mary Katherine BradfordDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218.
Karen WhitworthDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218.
Beverly WendlandDepartment of Biology, Johns Hopkins University, Baltimore, MD 21218 bwendland@jhu.edu.
Johns Hopkins University · US

Funding

MOLECULAR ANALYSIS OF ENDOCYTOSIS PROTEINS IN YEASTR01GM060979 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WENDLAND, BEVERLY R · 2000 to 2013
$4.3M
NIGMS NIH HHS R01 GM060979NIGMS NIH HHS R01 GM60979PHS HHS T32 007231-37
6 · The paper itself

Abstract

Endocytosis is a well-conserved process by which cells invaginate small portions of the plasma membrane to create vesicles containing extracellular and transmembrane cargo proteins. Dozens of proteins and hundreds of specific binding interactions are needed to coordinate and regulate these events. Saccharomyces cerevisiae is a powerful model system with which to study clathrin-mediated endocytosis (CME). Pan1 is believed to be a scaffolding protein due to its interactions with numerous proteins that act throughout the endocytic process. Previous research characterized many Pan1 binding interactions, but due to Pan1's essential nature, the exact mechanisms of Pan1's function in endocytosis have been difficult to define. We created a novel Pan1-degron allele, Pan1-AID, in which Pan1 can be specifically and efficiently degraded in <1 h upon addition of the plant hormone auxin. The loss of Pan1 caused a delay in endocytic progression and weakened connections between the coat/actin machinery and the membrane, leading to arrest in CME. In addition, we determined a critical role for the central region of Pan1 in endocytosis and viability. The regions important for endocytosis and viability can be separated, suggesting that Pan1 may have a distinct role in the cell that is essential for viability.

Indexed as

Amino Acid MotifsClathrinEndocytosisMicrofilament ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsClathrinMicrofilament ProteinsPAN1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25631817
PMCPMC4454182
OpenAlexW2107419718

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.