Evidence map›Paper›PMID 33021503›Full record

ArticleActa crystallographica. Section D, Structural biology2020

Structure of CYRI-B (FAM49B), a key regulator of cellular actin assembly.

Elise Kaplan, Rachael Stone, Peter J Hume, Nicholas P Greene, Vassilis Koronakis

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 17 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

5 authors at 1 institution in 1 country.

Elise KaplanDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.ORCID 0000-0003-4985-1482
Rachael StoneDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.ORCID 0000-0002-3320-8073
Peter J HumeDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.ORCID 0000-0002-4064-4519
Nicholas P GreeneDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.ORCID 0000-0002-3631-0380
Vassilis KoronakisDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom.ORCID 0000-0002-1353-1092
University of Cambridge · GB

Funding

Medical Research Council MR/N000994/1Wellcome TrustWellcome Trust 101828/Z/13/Z
6 · The paper itself

Abstract

In eukaryotes, numerous fundamental processes are controlled by the WAVE regulatory complex (WRC) that regulates cellular actin polymerization, crucial for cell motility, cell-cell adhesion and epithelial differentiation. Actin assembly is triggered by interaction of the small GTPase Rac1 with CYFIP1, a key component of the WRC. Previously known as FAM49B, CYRI-B is a protein that is highly conserved across the Eukaryota and has recently been revealed to be a key regulator of Rac1 activity. Mutation of CYRI-B or alteration of its expression therefore leads to altered actin nucleation dynamics, with impacts on lamellipodia formation, cell migration and infection by intracellular pathogens. In addition, knockdown of CYRI-B expression in cancer cell lines results in accelerated cell proliferation and invasiveness. Here, the structure of Rhincodon typus (whale shark) CYRI-B is presented, which is the first to be reported of any CYRI family member. Solved by X-ray crystallography, the structure reveals that CYRI-B comprises three distinct α-helical subdomains and is highly structurally related to a conserved domain present in CYFIP proteins. The work presented here establishes a template towards a better understanding of CYRI-B biological function.

Indexed as

AnimalsCrystallography, X-RayIntracellular Signaling Peptides and ProteinsMitochondrial ProteinsProtein Conformation, alpha-HelicalProtein DomainsSharksIntracellular Signaling Peptides and ProteinsMitochondrial Proteinsactin assemblycell-motility regulatorcrystal structureCYRI-BFAM49BSAD

Identifiers

PMID33021503
PMCPMC7543656
OpenAlexW3089109330

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.