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Formin binding protein 1

FBP17, formin-binding protein 17, FNBP1, Rapostlin, Formin binding protein 28
The protein encoded by this gene is a member of the formin-binding-protein family. The protein contains an N-terminal Fer/Cdc42-interacting protein 4 (CIP4) homology (FCH) domain followed by a coiled-coil domain, a proline-rich motif, a second coiled-coil domain, a Rho family protein-binding domain (RBD), and a C-terminal SH3 domain. This protein binds sorting nexin 2 (SNX2), tankyrase (TNKS), and dynamin; an interaction between this protein and formin has not been demonstrated yet in human. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Actin, beta 2-adrenoceptor, Src, CAN, Wasp
Papers using FBP17 antibodies
Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
Takenawa Tadaomi et al., In The Journal of Cell Biology, 2000
... Human FBP17 complementary DNA (cDNA) was cloned in pEGFP-C1 (CLONTECH Laboratories, Inc.) ...
Papers on FBP17
Preventing fibril formation of a protein by selective mutation.
Scheraga et al., Barcelona, Spain. In Proc Natl Acad Sci U S A, Dec 2015
The origins of formation of an intermediate state involved in amyloid formation and ways to prevent it are illustrated with the example of the Formin binding protein 28 (FBP28) WW domain, which folds with biphasic kinetics.
Translating Membrane Tension into Cytoskeletal Action by FBP17.
Friedl et al., Nijmegen, Netherlands. In Dev Cell, Jul 2015
They identify FBP17 as a multifunctional adaptor that senses membrane curvature and delivers feedback to actin dynamics and directed cell migration.
Feedback regulation between plasma membrane tension and membrane-bending proteins organizes cell polarity during leading edge formation.
Itoh et al., Kōbe, Japan. In Nat Cell Biol, Jun 2015
Here, we demonstrate that FBP17, a membrane-bending protein and an activator of WASP/N-WASP-dependent actin nucleation, is a PM tension sensor involved in leading edge formation.
Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.
Liwo et al., Wuhan, China. In Proc Natl Acad Sci U S A, 2015
To demonstrate the utility of the coarse-grained united-residue (UNRES) force field to compare experimental and computed kinetic data for folding proteins, we have performed long-time millisecond-timescale canonical Langevin molecular dynamics simulations of the triple β-strand from the Formin binding protein 28 WW domain and six nonnatural variants, using UNRES.
Interaction between Common Genetic Variants and Total Fat Intake on Low-Density Lipoprotein Peak Particle Diameter: A Genome-Wide Association Study.
Vohl et al., Québec, Canada. In J Nutrigenet Nutrigenomics, 2014
RESULTS: The GWAS analyses 29 identified independent SNP × total fat intake interaction effects on the LDL-PPD at p < 10(-5), including SNPs in the following genes: ABCG2, CPA3, FNBP1, KCNQ3, NBAS, NCALD, OPRL1, NKAIN2, SH3BGRL2, SOX5, and SUSD4.
Local vs global motions in protein folding.
Scheraga et al., Ithaca, United States. In J Chem Theory Comput, 2013
This question is addressed by analyzing folding and non-folding trajectories of a protein; as an example, the analysis is applied to the 37-residue triple β-strand WW domain from the Formin binding protein 28 (FBP28) (PDB ID: 1E0L).
Antagonistic regulation of F-BAR protein assemblies controls actin polymerization during podosome formation.
Takenawa et al., Kōbe, Japan. In J Cell Sci, 2013
FBP17, an F-BAR domain protein, has emerged as a crucial factor linking the plasma membrane to WASP-mediated actin polymerization.
Calcium oscillations-coupled conversion of actin travelling waves to standing oscillations.
De Camilli et al., New Haven, United States. In Proc Natl Acad Sci U S A, 2013
Recruitment of FBP17 and active Cdc42 at the plasma membrane, leading to actin polymerization, are involved in both events, whereas calcium oscillations, which correlate with global fluctuations of plasma membrane PI(4,5)P(2), are tightly linked to standing oscillations and counteract wave propagation.
Physicochemical analysis from real-time imaging of liposome tubulation reveals the characteristics of individual F-BAR domain proteins.
Takiguchi et al., Nagoya, Japan. In Langmuir, 2013
Here, we successfully monitored the entire process of tubulation and the behavior of elongated tubules caused by four different F-BAR domain family proteins (FBP17, CIP4, PSTPIP1, and Pacsin2) using direct real-time imaging of giant unilamellar liposomes with dark-field optical microscopy.
Membrane-deforming proteins play distinct roles in actin pedestal biogenesis by enterohemorrhagic Escherichia coli.
Welch et al., United States. In J Biol Chem, 2012
We found that three F-BAR proteins: CIP4, FBP17, and TOCA1 (transducer of Cdc42-dependent actin assembly), play different roles during actin pedestal biogenesis.
The F-BAR protein Rapostlin regulates dendritic spine formation in hippocampal neurons.
Negishi et al., Kyoto, Japan. In J Biol Chem, 2011
F-BAR protein Rapostlin, whose activity is regulated by Rnd2, plays a key role in spine formation through the regulation of membrane dynamics.
Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis.
Nichols et al., Cambridge, United Kingdom. In J Cell Sci, 2011
Overexpression of the F-BAR domain of pacsin 2 (but not the related F-BAR domains of CIP4 and FBP17) disrupts caveolar morphogenesis or trafficking, implying that pacsin 2 interacts with components required for these processes.
Coupling between clathrin-dependent endocytic budding and F-BAR-dependent tubulation in a cell-free system.
De Camilli et al., New Haven, United States. In Nat Cell Biol, 2010
Results suggest a functional link between FBP17-dependent membrane tubulation and clathrin-dependent budding. Clathrin spatially directs membrane invaginations that lead to the generation of endocytic vesicles larger than those enclosed by the coat.
Relation between free energy landscapes of proteins and dynamics.
Scheraga et al., Ithaca, United States. In J Chem Theory Comput, 2010
By examining the molecular dynamics (MD) of protein folding trajectories, generated with the coarse-grained UNRES force field, for the B-domain of staphylococcal protein A and the triple β-strand WW domain from the Formin binding protein 28 (FBP), by principal component analysis (PCA), it is demonstrated how different free energy landscapes (FELs) and folding pathways of trajectories can be, even though they appear to be very similar by visual inspection of the time-dependence of the root-mean-square deviation (rmsd).
FBP17 Mediates a Common Molecular Step in the Formation of Podosomes and Phagocytic Cups in Macrophages.
Ochs et al., Los Angeles, United States. In J Biol Chem, 2009
formin-binding protein 17 (FBP17) recruits WASP, WASP-interacting protein (WIP), and dynamin-2 to the plasma membrane and that this recruitment is necessary for the formation of podosomes and phagocytic cups.
EFC/F-BAR proteins and the N-WASP-WIP complex induce membrane curvature-dependent actin polymerization.
Suetsugu et al., Tokyo, Japan. In Embo J, 2008
N-WASP-WIP complex-mediated actin polymerization is activated by phosphatidylserine-containing membranes depending on membrane curvature in the presence of Toca-1 or FBP17 and in the absence of Cdc42 and phosphatidylinositol (4,5)-bisphosphate.
Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.
Yokoyama et al., Japan. In Cell, 2007
FBP17 is recruited to clathrin-coated pits in the late stage of endocytosis, indicating its physiological role.
Rho family GTPases and dendrite plasticity.
Katoh et al., Kyoto, Japan. In Neuroscientist, 2005
Rnd1 promotes spine maturation, and Rnd2 stimulates dendrite branching through its specific effector, Rapostlin.
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