Versatile membrane deformation potential of activated pacsin. [PDF]
Endocytosis is a fundamental process in signaling and membrane trafficking. The formation of vesicles at the plasma membrane is mediated by the G protein dynamin that catalyzes the final fission step, the actin cytoskeleton, and proteins that sense or ...
Shih Lin Goh +3 more
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Polarized hyphal growth of filamentous pathogenic fungi is an essential event for host penetration and colonization. The long-range early endosomal trafficking during hyphal growth is crucial for nutrient uptake, sensing of host-specific cues, and ...
Manisha Sinha +6 more
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FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular plate and regulate actin polymerization in vitro. [PDF]
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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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
PACSIN 1 forms tetramers via its N‐terminal F‐BAR domain [PDF]
The ability of protein kinase C and casein kinase 2 substrate in neurons (PACSIN)/syndapin proteins to self‐polymerize is crucial for the simultaneous interactions with more than one Src homology 3 domain‐binding partner or with lipid membranes. The assembly of this network has profound effects on the neural Wiskott–Aldrich syndrome protein‐mediated ...
Arndt, Halbach +5 more
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BAR Proteins PSTPIP1/2 Regulate Podosome Dynamics and the Resorption Activity of Osteoclasts. [PDF]
Bone resorption in vertebrates relies on the ability of osteoclasts to assemble F-actin-rich podosomes that condense into podosomal belts, forming sealing zones.
Martin Sztacho +5 more
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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
Simulation of Membrane Sculpting by EFC F-BAR Domain Lattices [PDF]
Cells, during cellular morphogenesis, are dynamically sculpted into different compartments by membranes with the help of proteins. The BAR domain is one of the conserved protein domains that is involved in shaping cellular membranes in vivo, and is observed to induce tubule formation from liposomes in vitro.
Yu, Hang +3 more
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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
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F-BAR/EFC Domain Proteins: Some Assembly Required [PDF]
Polymeric spirals of crescent-shaped BAR-domain superfamily proteins are touted to girdle eukaryotic phospholipid bilayers into narrow tubules for trafficking and membrane remodeling events. But McDonald et al. (2015) in this issue of Developmental Cell question whether this broadly held view and conceptually appealing mechanism for membrane sculpting ...
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