A Hinge in the Distal End of the PACSIN 2 F-BAR Domain May Contribute to Membrane-Curvature Sensing
Journal of Molecular Biology, 2010 The protein kinase C and casein kinase 2 substrates in neurons (PACSINs) represent a subfamily of membrane-binding proteins characterized by an amino-terminal Bin-Amphiphysin-Rvs (F-BAR) domain. PACSINs link membrane trafficking with actin dynamics and regulate the localization of distinct cargo molecules.
Plomann, Markus +2 more
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F-BAR domain proteins: Families and function. [PDF]
Commun Integr Biol, 2010 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
Ahmed S +4 more
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Phospholipid binding residues of eukaryotic membrane-remodelling F-BAR domain proteins are conserved in Helicobacter pylori CagA. [PDF]
BMC Res Notes, 2014 Background: 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
Roujeinikova A.
europepmc +2 more sources
Coordinated autoinhibition of F-BAR domain membrane binding and WASp activation by Nervous Wreck. [PDF]
Proc Natl Acad Sci U S A, 2016 Significance Membrane-deforming proteins cooperate with the cytoskeleton to sculpt lipid bilayers into complex and dynamic geometries, but we still do not understand how their activities are temporally and spatially regulated in cells.
Stanishneva-Konovalova TB +6 more
europepmc +4 more sources
Characterization of the EFC/F-BAR domain protein, FCHO2 [PDF]
Genes to Cells, 2011 We have previously shown that SGIP1α is an endocytic protein specifically expressed in neural tissues. SGIP1α has a lipid-binding domain called the MP domain, which shows no significant homology to any other domains. In this study, we characterized FCHO2, a protein with a high level of homology to SGIP1α. FCHO2 lacks the MP domain but has another lipid-
Akiyoshi Uezu +5 more
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Structural Basis of Membrane Invagination by F-BAR Domains [PDF]
Cell, 2008 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
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F-BAR domains: multifunctional regulators of membrane curvature [PDF]
Journal of Cell Science, 2008 The F-BAR-domain-containing proteins (F-BAR proteins) are a group of adaptor proteins, members of which are found in all eukaryotes except plants. Also known as Pombe/Cdc15 homology (PCH)-family proteins, they have essential roles in fundamental biological processes, such as endocytosis ...
Robert J W, Heath, Robert H, Insall
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FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets. [PDF]
Blood, 2015 Key PointsThe F-BAR protein PACSIN2 associates with the initiating demarcation membrane system in megakaryocytes. FlnA binding to the PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes, platelets, and in vitro.
Begonja AJ +13 more
europepmc +4 more sources
Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site. [PDF]
Structure, 2015 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
FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular plate and regulate actin polymerization in vitro. [PDF]
PLoS ONE, 2013 Mammalian FCHSD1 and FCHSD2 are homologous proteins containing an amino-terminal F-BAR domain and two SH3 domains near their carboxyl-termini. We report here that FCHSD1 and FCHSD2 are expressed in mouse cochlear sensory hair cells.
Huiren Cao +9 more
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