Crystal Structure of the Epo1-Bem3 Complex for Bud Growth.

Jin Wang, Lei Li, Zhenhua Ming, Lijie Wu, Liming Yan

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Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact, top 97% 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

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3 · Its place in the literature

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0 citing papers in PubMed, 1 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors at 4 institutions in 1 country.

Jin WangState Key Laboratory of Biotherapy, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu 610041, China.ORCID 0000-0003-1593-9056

Lei LiState Key Laboratory of Biotherapy, West China Hospital, Collaborative Innovation Center for Biotherapy, Sichuan University, Chengdu 610041, China.

Zhenhua MingState Key Laboratory for Conservation and Utilization of Subtropical Agro-Bioresources, College of Life Science and Technology, Guangxi University, Nanning 530000, China.

Lijie WuiHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Liming YanLaboratory of Structural Biology and MOE Laboratory of Protein Science, School of Medicine, Tsinghua University, Beijing 100084, China.ORCID 0000-0003-0648-9604

Sichuan University · CNGuangxi University · CNShanghaiTech University · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubules of the endoplasmic reticulum (ER) spread into the buds of yeast by an actin-based mechanism and, upon entry, become attached to the polarisome, a proteinaceous micro-compartment below the tip of the bud. The minimal tether between polarisome and cortical ER is formed by a protein complex consisting of Epo1, a member of the polarisome, Scs2, a membrane protein of the ER and Cdc42 guanosine triphosphatase-activating protein Bem3. Here, we report the crystal structure of a complex between Epo1 and Bem3. In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1. Our findings provide a first structural insight into the molecular architecture of the link between cortical ER and the polarisome.

Indexed as

Models, MolecularProtein ConformationSaccharomyces cerevisiaeAmino Acid SequenceCarrier ProteinsCrystallography, X-RayGTPase-Activating ProteinsMagnetic Resonance SpectroscopyMultiprotein ComplexesProtein BindingProtein MultimerizationSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipBEM3 protein, S cerevisiaeCarrier ProteinsEpo1 protein, S cerevisiaeGTPase-Activating ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteinsbudding yeastcomplexEpo1-Bem3polarisomeSsc2

Identifiers

PMID33917059

DOI10.3390/ijms22083812

PMCPMC8067709

OpenAlexW3142230685

What OpenQuestion holds

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LicenceCC BY

Read underepoch 390

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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.