Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1.
about
Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?Actin nucleators in the nucleus: an emerging themeTargeting and transport: how microtubules control focal adhesion dynamicsFormins at a glanceCommon formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.Automated screening of microtubule growth dynamics identifies MARK2 as a regulator of leading edge microtubules downstream of Rac1 in migrating cellsCytoplasmic dynamics of the general nuclear import machinery in apically growing syncytial cellsMicrotubules as platforms for assaying actin polymerization in vivoMolecular Basis of Actin Nucleation Factor Cooperativity: CRYSTAL STRUCTURE OF THE SPIR-1 KINASE NON-CATALYTIC C-LOBE DOMAIN (KIND){middle dot}FORMIN-2 FORMIN SPIR INTERACTION MOTIF (FSI) COMPLEXMechanism of actin filament nucleation by Vibrio VopL and implications for tandem W domain nucleationStructure of the formin-interaction domain of the actin nucleation-promoting factor Bud6The Bacterial Effector VopL Organizes Actin into Filament-like StructuresThe F-BAR protein Hof1 tunes formin activity to sculpt actin cables during polarized growth.Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleationThe APC tumor suppressor is required for epithelial cell polarization and three-dimensional morphogenesisMitogen-activated protein kinase (MAPK/ERK) regulates adenomatous polyposis coli during growth-factor-induced cell extensionGlyceraldehyde 3-phosphate dehydrogenase is required for band 3 (anion exchanger 1) membrane residency in the mammalian kidneyAn mDia1-INF2 formin activation cascade facilitated by IQGAP1 regulates stable microtubules in migrating cells.Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1Tumorigenic fragments of APC cause dominant defects in directional cell migration in multiple model systemsRocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging.Direct interaction between two actin nucleators is required in Drosophila oogenesis.Profilin connects actin assembly with microtubule dynamics.Dissecting regulatory networks of filopodia formation in a Drosophila growth cone modelCellular control of cortical actin nucleation.The tumor suppressor adenomatous polyposis coli controls the direction in which a cell extrudes from an epitheliumE-cadherin and the cytoskeletal network in colorectal cancer development and metastasis.Self-association of the APC tumor suppressor is required for the assembly, stability, and activity of the Wnt signaling destruction complex.APC/β-catenin-rich complexes at membrane protrusions regulate mammary tumor cell migration and mesenchymal morphologyNew mechanisms and functions of actin nucleationSmall molecule inhibitor of formin homology 2 domains (SMIFH2) reveals the roles of the formin family of proteins in spindle assembly and asymmetric division in mouse oocytesMechanism and cellular function of Bud6 as an actin nucleation-promoting factor.Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.Molecular architecture of the Spire-actin nucleus and its implication for actin filament assemblyDestruction complex function in the Wnt signaling pathway of Drosophila requires multiple interactions between Adenomatous polyposis coli 2 and ArmadilloStructure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment MotifAPC binds the Miro/Milton motor complex to stimulate transport of mitochondria to the plasma membraneAPC binds intermediate filaments and is required for their reorganization during cell migration.Drosophila homologues of adenomatous polyposis coli (APC) and the formin diaphanous collaborate by a conserved mechanism to stimulate actin filament assembly.The WH2 Domain and Actin Nucleation: Necessary but Insufficient
P2860
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P2860
Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@ast
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@en
type
label
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@ast
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@en
prefLabel
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@ast
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@en
P2093
P2860
P356
P1476
Adenomatous polyposis coli pro ...... ergizes with the formin mDia1.
@en
P2093
Bruce L Goode
Francesca Bartolini
Gregg G Gundersen
James B Moseley
Kyoko Okada
Zvonimir Dogic
P2860
P304
P356
10.1083/JCB.201001016
P407
P577
2010-06-21T00:00:00Z