The State of F-BAR Domains as Membrane-Bound Oligomeric Platforms [PDF]
Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains, like all BAR domains, are dimeric units that oligomerize and bind membranes. F-BAR domains are generally coupled to additional domains that function in protein binding or have enzymatic activity.
Kathleen Gould +2 more
exaly +4 more sources
Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation [PDF]
Members of the Bin/amphiphysin/Rvs (BAR) domain protein superfamily are involved in membrane remodeling in various cellular pathways ranging from endocytic vesicle and T-tubule formation to cell migration and neuromorphogenesis. Membrane curvature induction and stabilization are encoded within the BAR or Fer-CIP4 homology-BAR (F-BAR) domains, α-helical
Rao, Yijian +9 more
openaire +6 more sources
The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially regulate membrane deformation [PDF]
Coordination of membrane deformation and cytoskeletal dynamics lies at the heart of many biological processes critical for cell polarity, motility and morphogenesis. We recently showed that slit-robo GTPase-activating protein 2 (srGAP2) regulates neuronal morphogenesis through the ability of its F-BAR domain to regulate membrane deformation and induce ...
Jaeda, Coutinho-Budd +3 more
openaire +4 more sources
Role of the F-BAR Family Member PSTPIP2 in Autoinflammatory Diseases. [PDF]
Proline-serine-threonine-phosphatase-interacting protein 2 (PSTPIP2) belongs to the Fes/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain family. It exhibits lipid-binding, membrane deformation, and F-actin binding activity, suggesting broader roles at the membrane–cytoskeleton interface.
Xu JJ +6 more
europepmc +5 more sources
On the Trichoptera of Italy with delineation of incipient sibling species [PDF]
Lumpers, focussing between gross and molecular morphologies and neglecting fine phenomics, highly underesti-mate biodiversity. The outdated lumper’s attitude fixed in the Distribution Atlas of European Trichoptera (Neu et al.
Oláh, János +2 more
doaj +1 more source
Setting the F-BAR: Functions and regulation of the F-BAR protein family [PDF]
F-BAR domain proteins serve as transient linkers between the cell cortex and the cytoskeleton in multiple biological contexts. Recent studies have detailed roles for this protein family in endocytosis, cytokinesis, neurotransmission, motility and cellular morphogenesis. Here, we review emerging functional information regarding the recently recognized F-
Rachel H, Roberts-Galbraith +1 more
openaire +2 more sources
Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis [PDF]
Cytokinesis is a highly ordered cellular process driven by interactions between central spindle microtubules and the actomyosin contractile ring linked to the dynamic remodelling of the plasma membrane.
Tetsuya Takeda +6 more
doaj +1 more source
Direct interaction of actin filaments with F-BAR protein pacsin2. [PDF]
Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes.
Kostan J +18 more
europepmc +5 more sources
The F-BAR domain is emerging as an important player in membrane remodeling pathways. F-BAR domain proteins couple membrane remodeling with actin dynamics associated with endocytic pathways and filopodium formation. Here, we provide a comprehensive analysis of F-BAR domain proteins in terms of their evolutionary relationships and protein function. F-BAR
Sohail, Ahmed +4 more
openaire +2 more sources
Linking up at the BAR: Oligomerization and F-BAR protein function. [PDF]
As cells grow, move, and divide, they must reorganize and rearrange their membranes and cytoskeleton. The F-BAR protein family links cellular membranes with actin cytoskeletal rearrangements in processes including endocytosis, cytokinesis, and cell motility.
McDonald NA, Gould KL.
europepmc +4 more sources

