FMNL3 FH2–actin structure gives insight into formin-mediated actin nucleation and elongation

被引：0

作者：

Morgan E Thompson

Ernest G Heimsath

Timothy J Gauvin

Henry N Higgs

F Jon Kull

机构：

[1] Geisel School of Medicine at Dartmouth,Department of Biochemistry

[2] Dartmouth College,Department of Chemistry

来源：

Nature Structural & Molecular Biology | 2013年 / 20卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

摘要：

Formins regulate actin nucleation and filament elongation through their conserved FH2 domain. The formin FMNL3 induces assembly of filopodia, and now the crystal structure of its FH2 domain in complex with actin, together with functional analyses, provides insight into formin's activities.

引用

页码：111 / 118

页数：7

共 43 条

[21] Arp2/3 complex- and formin-mediated actin cytoskeleton networks facilitate actin binding protein sorting in fission yeast
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[23] Regulation of actin dynamics by the formin FMNL3 requires the C-terminus: Relationship to the formins INF2 and mDia1
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[24] An alternative splice isoform of the formin FMNL1 contributes to cancer cell adhesion and migration independent of the actin-binding ability of the FH2 domain.
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[25] Actin Polymerization by the Formin Fmnl3 Supports Epithelial Cell-Cell Junction Integrity during Collective Cell Migration
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MOLECULAR BIOLOGY OF THE CELL, 2017, 28
[27] Arp2/3 complex- and formin-mediated actin networks tune actin-binding protein sorting in fission yeast.
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Calabrese, B.
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Higgs, H. N.
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MOLECULAR BIOLOGY OF THE CELL, 2015, 26
[29] The C Terminus of Formin FMNL3 Accelerates Actin Polymerization and Contains a WH2 Domain-like Sequence That Binds Both Monomers and Filament Barbed Ends
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JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (05) : 3087 - 3098
[30] Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation
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JOURNAL OF CELL SCIENCE, 2003, 116 (22) : 4567 - 4575

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