Evidence map›Paper›PMID 36028485›Full record

ArticleNature communications2022

Multivalent interactions between molecular components involved in fast endophilin mediated endocytosis drive protein phase separation.

Samsuzzoha Mondal, Karthik Narayan, Samuel Botterbusch, Imania Powers, Jason Zheng, Honey Priya James, Rui Jin, Tobias Baumgart

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
8.2field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 74 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Samsuzzoha MondalDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0002-2612-5974
Karthik NarayanDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0003-1047-0375
Samuel BotterbuschDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0002-1593-6069
Imania PowersDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Jason ZhengDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.ORCID 0000-0001-6652-7022
Honey Priya JamesDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Rui JinDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA.
Tobias BaumgartDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA, 19104, USA. baumgart@sas.upenn.edu.ORCID 0000-0001-7385-8460
University of Pennsylvania · US

Funding

Membrane shape transition control in cellular membrane trafficking phenomenaR01GM097552 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BAUMGART, TOBIAS · 2011 to 2023
$4.5M
NIGMS NIH HHS R01 GM097552
6 · The paper itself

Abstract

A specific group of transmembrane receptors, including the β1-adrenergic receptor (β1-AR), is internalized through a non-clathrin pathway known as Fast Endophilin Mediated Endocytosis (FEME). A key question is: how does the endocytic machinery assemble and how is it modulated by activated receptors during FEME. Here we show that endophilin, a major regulator of FEME, undergoes a phase transition into liquid-like condensates, which facilitates the formation of multi-protein assemblies by enabling the phase partitioning of endophilin binding proteins. The phase transition can be triggered by specific multivalent binding partners of endophilin in the FEME pathway such as the third intracellular loop (TIL) of the β1-AR, and the C-terminal domain of lamellipodin (LPD). Other endocytic accessory proteins can either partition into, or target interfacial regions of, these condensate droplets, and LPD also phase separates with the actin polymerase VASP. On the membrane, TIL promotes protein clustering in the presence of endophilin and LPD C-terminal domain. Our results demonstrate how the multivalent interactions between endophilin, LPD, and TIL regulate protein assembly formation on the membrane, providing mechanistic insights into the priming and initiation steps of FEME.

Indexed as

ActinsEndocytosisCarrier ProteinsSignal TransductionActinsCarrier Proteins

Identifiers

PMID36028485
PMCPMC9418313
OpenAlexW4293199651

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.