Acta Crystallogr D Struct Biol October 2020 PMID 33021503

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

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

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Peak: 2 in Sep 2020

across 2 sources since Sep 2020

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Sep 2020 – Apr 2021

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AI synopsis

What people are saying

The discussions highlight the structural insights provided by the study, with posts stressing the protein's role in cell movement and its structural similarity to other key components, reflecting a knowledgeable tone that underscores the research's relevance and potential for advancing understanding of cellular processes.

AgreementModerate agreement

Most posts recognize the importance of the study, with some explicitly acknowledging it as a key regulator of actin assembly, indicating general consensus on its significance.

InterestHigh interest

The discussions demonstrate high interest, referencing specific details like structure and regulation, showing curiosity about the biological implications.

EngagementModerate engagement

Posts include mentions of structural analysis and the broader role in cell motility, suggesting active engagement and some technical understanding.

ImpactModerate impact

While not universally described as transformative, posts imply that understanding CYRI-B’s structure could influence future research in cell biology and disease, indicating moderate perceived impact.

Abstract in brief

The text explains that CYRIB, also known as FAM49B, is a highly conserved protein in eukaryotes that plays a crucial role in regulating actin assembly by interacting with Rac1, which affects cell movement, adhesion, and differentiation.
Mutations or changes in CYRIB expression can disrupt actin dynamics, influencing processes like cell migration, formation of structures like lamellipodia, and susceptibility to infections; in cancer cells, reduced CYRIB can lead to increased proliferation and invasiveness.
The study reports the crystal structure of CYRIB from whale sharks, revealing it has three helical domains and is structurally similar to parts of the WRC component CYFIP, which helps in understanding CYRIB's biological functions.]

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Structure and Regulation of CYRI-B in Actin Assembly

CYRI-B, also known as FAM49B, is a conserved protein crucial for actin assembly regulation through interactions with Rac1. Its structure, comprising three helical domains, offers insights into its role in cell motility…

International Union of Crystallography · Apr 15, 2021 24 views

CYRI-B Structural Insights and Role in Cellular Actin Regulation

This video discusses the crystal structure of CYRI-B, a conserved protein crucial for regulating actin assembly through Rac1 interaction, impacting cell motility, adhesion, and cancer cell behavior, based on structural…

International Union of Crystallography · Apr 15, 2021 11 views

Structural Biology

@ActaCrystD · X

RT @Diamond_MX: New Paper from I04 in @ActaCrystD https://t.co/NHgkh7sso0 (https://t.co/oGSgSkOzTa)

Oct 16, 2020 · 2 shares · 3,021 followers View post →

Diamond MX Beamlines

@Diamond_MX · X

New Paper from I04 in @ActaCrystD https://t.co/NHgkh7sso0 (https://t.co/oGSgSkOzTa)

Oct 16, 2020 · 1 like · 2 shares · 1,424 followers View post →

African Synchrotron

@AfSynchrotron · X

Structure of CYRI-B (FAM49B), a key regulator of cellular actin assembly https://t.co/sPCWjPjDvh via @ActaCrystD https://t.co/tup5Gcd2LE

Sep 30, 2020 · 2,922 followers View post →