Journal:Acta Cryst D:S2059798320010906
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | CYRI-B, also called FAM49B, is a well-conserved eukaryotic protein which interacts with the small GTPase Rac1 to regulate cellular actin assembly [1,2]<ref name="Shang1">PMID:29632189</ref><ref name="Fort2">PMID:30250061</ref>. Through its interaction with Rac1, CYRI-B controls multiple critical cellular functions including T cell activation [1]<ref name="Shang1">PMID:29632189</ref>, chemotaxis and cell migration [2,3]<ref name="Fort2">PMID:30250061</ref><ref name="Whitelaw3">PMID:31413787</ref>. CYRI-B has also been described to reduce cellular entry of several bacterial pathogens [4] and has been suggested to play a role in various cancers [5, 6]. | + | CYRI-B, also called FAM49B, is a well-conserved eukaryotic protein which interacts with the small GTPase Rac1 to regulate cellular actin assembly [1,2]<ref name="Shang1">PMID:29632189</ref><ref name="Fort2">PMID:30250061</ref>. Through its interaction with Rac1, CYRI-B controls multiple critical cellular functions including T cell activation [1]<ref name="Shang1">PMID:29632189</ref>, chemotaxis and cell migration [2,3]<ref name="Fort2">PMID:30250061</ref><ref name="Whitelaw3">PMID:31413787</ref>. CYRI-B has also been described to reduce cellular entry of several bacterial pathogens [4]<ref name="Yuki4">PMID:31285585</ref> and has been suggested to play a role in various cancers [5, 6]<ref name="Long5">PMID:29059164</ref><ref name="Chen6">PMID:31010678</ref>. |
| - | The structure of CYRI-B has been solved by X-ray crystallography at 2.4 Å resolution. It reveals an entirely α-helical protein organised into three distinct subdomains. The CYRI-B structure exhibits significant similarity with a conserved domain of CYFIP1, a key component of the WAVE regulatory complex (WRC) that interacts with Rac1 to promote actin polymerisation [7]. The study highlights residues crucial for Rac1 binding in both proteins. This suggests that CYRI-B interacts with Rac1 in the same manner as CYFIP1, regulating actin dependent processes by competition with the WRC for Rac1 binding. The structure provides a better understanding of the many roles played by CYRI-B, and also by other members of the CYRI protein family, in eukaryotic cells. | + | The structure of CYRI-B has been solved by X-ray crystallography at 2.4 Å resolution. It reveals an entirely α-helical protein organised into three distinct subdomains. The CYRI-B structure exhibits significant similarity with a conserved domain of CYFIP1, a key component of the WAVE regulatory complex (WRC) that interacts with Rac1 to promote actin polymerisation [7]<ref name="Chen7">PMID:21107423</ref>. The study highlights residues crucial for Rac1 binding in both proteins. This suggests that CYRI-B interacts with Rac1 in the same manner as CYFIP1, regulating actin dependent processes by competition with the WRC for Rac1 binding. The structure provides a better understanding of the many roles played by CYRI-B, and also by other members of the CYRI protein family, in eukaryotic cells. |
References | References | ||
Revision as of 12:54, 24 August 2020
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
