Results 21 to 30 of about 10,499,655 (247)

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

Cdk1-dependent phosphoinhibition of a formin-F-BAR interaction opposes cytokinetic contractile ring formation. [PDF]

open access: yesMol Biol Cell, 2018
In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). A single essential formin, Cdc12, localizes to the cell middle upon mitotic onset and nucleates the F-actin of the CR.
Willet AH, Bohnert KA, Gould KL.
europepmc   +2 more sources

F-BAR domain proteins: Families and function. [PDF]

open access: yesCommun 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
europepmc   +4 more sources

Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation [PDF]

open access: yesCell Reports, 2015
F-BAR domain proteins regulate and sense membrane curvature by interacting with negatively charged phospholipids and assembling into higher-order scaffolds. However, regulatory mechanisms controlling these interactions are poorly understood.
Charlotte F. Kelley   +12 more
doaj   +2 more sources

The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions. [PDF]

open access: yesNat Commun, 2016
Vascular homoeostasis, development and disease critically depend on the regulation of endothelial cell–cell junctions. Here we uncover a new role for the F-BAR protein pacsin2 in the control of VE-cadherin-based endothelial adhesion. Pacsin2 concentrates
Dorland YL   +13 more
europepmc   +2 more sources

A Cdc42 GEF, Gef1, through endocytosis organizes F-BAR Cdc15 along the actomyosin ring and promotes concentric furrowing.

open access: yesJ Cell Sci, 2019
During cytokinesis, fission yeast coordinates actomyosin ring constriction with septum ingression, resulting in concentric furrow formation by a poorly defined mechanism.
Onwubiko UN   +6 more
europepmc   +2 more sources

OCRL1 engages with the F-BAR protein pacsin 2 to promote biogenesis of membrane-trafficking intermediates. [PDF]

open access: yesMol Biol Cell, 2016
The Lowe syndrome protein OCRL1 binds via IPIP27A to the F-BAR protein pacsin 2 to promote the biogenesis of trafficking intermediates containing the mannose 6-phosphate receptor at the trans-Golgi network and endosomes.
Billcliff PG   +6 more
europepmc   +2 more sources

F-BAR family proteins, emerging regulators for cell membrane dynamic changes-from structure to human diseases. [PDF]

open access: yesJ Hematol Oncol, 2015
Eukaryotic cell membrane dynamics change in curvature during physiological and pathological processes. In the past ten years, a novel protein family, Fes/CIP4 homology-Bin/Amphiphysin/Rvs (F-BAR) domain proteins, has been identified to be the most ...
Liu S, Xiong X, Zhao X, Yang X, Wang H.
europepmc   +2 more sources

Assembly of actin filaments and microtubules in Nwk F-BAR-induced membrane deformations. [PDF]

open access: yesCommun Integr Biol, 2015
F-BAR domains form crescent-shaped dimers that bind to and deform lipid bilayers, and play a role in many cellular processes requiring membrane remodeling, including endocytosis and cell morphogenesis.
Kelley CF   +4 more
europepmc   +2 more sources

The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12. [PDF]

open access: yesJ Cell Biol, 2015
Cdc15 contributes to contractile ring formation and cytokinesis by recruiting the formin Cdc12, which defines a novel cytokinetic function for an F-BAR domain.
Willet AH   +6 more
europepmc   +2 more sources

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