Results 21 to 30 of about 1,206,903 (162)

Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity [PDF]

open access: yesCellular and Molecular Life Sciences
Polarized cell growth necessitates the dynamic remodeling of the plasma membrane, a process requiring BAR domain-containing proteins. While classical BAR proteins, with their crescent-shaped structure, are well characterized, the mechanisms underlying ...
Biyu Zheng   +11 more
doaj   +2 more sources

Characterization of the EFC/F-BAR domain protein, FCHO2. [PDF]

open access: yesGenes to cells : devoted to molecular & cellular mechanisms, 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
openaire   +3 more sources

F-BAR domains: multifunctional regulators of membrane curvature [PDF]

open access: yesJournal 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
openaire   +2 more sources

Comparative Study of Curvature Sensing Mediated by F-BAR and an Intrinsically Disordered Region of FBP17

open access: yesiScience, 2020
Summary: Membrane curvature has emerged as an intriguing physical principle underlying biological signaling and membrane trafficking. The CIP4/FBP17/Toca-1 F-BAR subfamily is unique in the BAR family because its structurally folded F-BAR domain does not ...
Maohan Su   +6 more
doaj   +1 more source

“Wunder” F-BAR Domains: Going from Pits to Vesicles [PDF]

open access: yesCell, 2007
Clathrin-mediated endocytosis is a key mechanism by which cells take up extracellular cargo. In this issue, Shimada et al. (2007) reveal the mode of action of the F-BAR domain, which deepens the initial membrane pit that forms during clathrin-mediated endocytosis.
Fütterer, Klaus, Machesky, Laura M.
openaire   +2 more sources

Versatile membrane deformation potential of activated pacsin. [PDF]

open access: yesPLoS ONE, 2012
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
doaj   +1 more source

Modulation of fungal virulence through CRZ1 regulated F-BAR-dependent actin remodeling and endocytosis in chickpea infecting phytopathogen Ascochyta rabiei.

open access: yesPLoS Genetics, 2021
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
doaj   +1 more source

FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular plate and regulate actin polymerization in vitro. [PDF]

open access: yesPLoS 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
doaj   +1 more source

PACSIN 1 forms tetramers via its N‐terminal F‐BAR domain [PDF]

open access: yesThe FEBS Journal, 2007
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
openaire   +2 more sources

BAR Proteins PSTPIP1/2 Regulate Podosome Dynamics and the Resorption Activity of Osteoclasts. [PDF]

open access: yesPLoS ONE, 2016
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
doaj   +1 more source

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