Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
about
An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2Heading off with the herd: how cancer cells might maneuver supernumerary centrosomes for directional migrationFormins at a glanceMammalian diaphanous-related formin 1 regulates GSK3β-dependent microtubule dynamics required for T cell migratory polarizationSmall-molecule agonists of mammalian Diaphanous-related (mDia) formins reveal an effective glioblastoma anti-invasion strategy.Maytansine-loaded star-shaped folate-core PLA-TPGS nanoparticles enhancing anticancer activityAn mDia1-INF2 formin activation cascade facilitated by IQGAP1 regulates stable microtubules in migrating cells.INF2 promotes the formation of detyrosinated microtubules necessary for centrosome reorientation in T cellsActin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1An optogenetic tool for the activation of endogenous diaphanous-related formins induces thickening of stress fibers without an increase in contractilityThe role of formin tails in actin nucleation, processive elongation, and filament bundling.Accelerated actin filament polymerization from microtubule plus ends.SMIFH2 has effects on Formins and p53 that perturb the cell cytoskeletonSplice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture.Connecting the cytoskeleton to the endoplasmic reticulum and Golgi.Novel roles for actin in mitochondrial fissionThe ability to induce microtubule acetylation is a general feature of formin proteins.Small 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 oocytesProteomic analyses uncover a new function and mode of action for mouse homolog of Diaphanous 2 (mDia2)Structural insights into WHAMM-mediated cytoskeletal coordination during membrane remodeling.Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing.Reorganization of actin filaments by ADF/cofilin is involved in formation of microtubule structures during Xenopus oocyte maturation.Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope.Control of myofibroblast differentiation by microtubule dynamics through a regulated localization of mDia2mDia1 regulates breast cancer invasion by controlling membrane type 1-matrix metalloproteinase localization.Actin monomers activate inverted formin 2 by competing with its autoinhibitory interaction.The formin protein mDia2 serves as a marker of spindle pole dynamics in vitrified-warmed mouse oocytesInteraction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly.Essential and nonredundant roles for Diaphanous formins in cortical microtubule capture and directed cell migration.Formin' cellular structures: Physiological roles of Diaphanous (Dia) in actin dynamics.New insights into the role of plant formins: regulating the organization of the actin and microtubule cytoskeleton.The role of membrane rafts in Lck transport, regulation and signalling in T-cells.Bacterial subversion of host cytoskeletal machinery: hijacking formins and the Arp2/3 complex.Neuropathologic characterization of INF2-related Charcot-Marie-Tooth disease: evidence for a Schwann cell actinopathy.Splitting up the powerhouse: structural insights into the mechanism of mitochondrial fission.The formin DAAM is required for coordination of the actin and microtubule cytoskeleton in axonal growth cones.DIAPH3 governs the cellular transition to the amoeboid tumour phenotype.Mammalian Diaphanous-related formin-1 restricts early phases of influenza A/NWS/33 virus (H1N1) infection in LLC-MK2 cells by affecting cytoskeleton dynamics.OsFH15, a class I formin, interacts with microfilaments and microtubules to regulate grain size via affecting cell expansion in rice.Centrosome polarization in T cells: a task for formins
P2860
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P2860
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@ast
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@en
type
label
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@ast
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@en
prefLabel
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@ast
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@en
P2093
P2860
P356
P1476
Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules.
@en
P2093
Emmanuelle Neumanne
Jeremie Gaillard
Marylin Vantard
Pinar Gurel
Vinay Ramabhadran
P2860
P304
P356
10.1091/MBC.E11-07-0616
P577
2011-10-12T00:00:00Z