Structural Basis of Membrane Invagination by F-BAR Domains [PDF]
BAR superfamily domains shape membranes through poorly understood mechanisms. We solved structures of F-BAR modules bound to flat and curved bilayers using electron (cryo)microscopy. We show that membrane tubules form when F-BARs polymerize into helical coats that are held together by lateral and tip-to-tip interactions. On gel-state membranes or after
Frost, Adam +7 more
openaire +4 more sources
A proof of strong normalisation using domain theory [PDF]
Ulrich Berger presented a powerful proof of strong normalisation using domains, in particular it simplifies significantly Tait's proof of strong normalisation of Spector's bar recursion.
Thierry Coquand, Arnaud Spiwack
doaj +15 more sources
Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site. [PDF]
F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although they are generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of F-BAR domains are functionally important.
Moravcevic K +6 more
europepmc +4 more sources
Strong normalisation for applied lambda calculi [PDF]
We consider the untyped lambda calculus with constructors and recursively defined constants. We construct a domain-theoretic model such that any term not denoting bottom is strongly normalising provided all its `stratified approximations' are.
Ulrich Berger
doaj +6 more sources
The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesis. [PDF]
Robust cell–cell adhesion is critical for tissue integrity and morphogenesis, yet little is known about the molecular mechanisms controlling cell–cell junction architecture and strength. We discovered that SRGP-1 is a novel component of cell–cell junctions in Caenorhabditis elegans, localizing via its F-BAR (Bin1, Amphiphysin, and RVS167) domain and a ...
Zaidel-Bar R +5 more
europepmc +4 more sources
Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation. [PDF]
Syndapin I (PACSIN 1) is a synaptically enriched membrane tubulating protein that plays important roles in activity-dependent bulk endocytosis and neuronal morphogenesis. While syndapin I is an in vitro phosphoprotein, it is not known to be phosphorylated in neurons.
Quan A +8 more
europepmc +6 more sources
The inverse F-BAR domain protein srGAP2 acts through srGAP3 to modulate neuronal differentiation and neurite outgrowth of mouse neuroblastoma cells. [PDF]
The inverse F-BAR (IF-BAR) domain proteins srGAP1, srGAP2 and srGAP3 are implicated in neuronal development and may be linked to mental retardation, schizophrenia and seizure.
Yue Ma +5 more
doaj +2 more sources
Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II. [PDF]
Caveolae are flask-shaped invaginations of the plasma membrane. The BAR domain proteins form crescent-shaped dimers, and their oligomeric filaments are considered to form spirals at the necks of invaginations, such as clathrin-coated pits and caveolae.
Senju Y, Suetsugu S.
europepmc +4 more sources
Phospholipid binding residues of eukaryotic membrane-remodelling F-BAR domain proteins are conserved in Helicobacter pylori CagA. [PDF]
Cytotoxin associated gene product A (CagA) is an oncogenic protein secreted by the gastric bacterium Helicobacter pylori. Internalization of CagA by human epithelial cells occurs by an unknown mechanism that requires interaction with the host membrane lipid phosphatidylserine.Local homology at the level of amino acid sequence and secondary structure ...
Roujeinikova A.
europepmc +4 more sources
The F-BAR Domain of srGAP2 Induces Membrane Protrusions Required for Neuronal Migration and Morphogenesis [PDF]
During brain development, proper neuronal migration and morphogenesis is critical for the establishment of functional neural circuits. Here we report that srGAP2 negatively regulates neuronal migration and induces neurite outgrowth and branching through the ability of its F-BAR domain to induce filopodia-like membrane protrusions resembling those ...
Guerrier, Sabrice +8 more
openaire +4 more sources

