Results 11 to 20 of about 13,129,737 (272)

Small GTPase Cdc42, WASP, and scaffold proteins for higher-order assembly of the F-BAR domain protein. [PDF]

Sci Adv, 2023
The higher-order assembly of Bin-amphiphysin-Rvs (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, into lattice on the membrane is essential for the formation of subcellular structures. However, the regulation of their ordered assembly has not been elucidated.
Wan Mohamad Noor WNI, Nguyen NTH, Cheong TH, Chek MF, Hakoshima T, Inaba T, Hanawa-Suetsugu K, Nishimura T, Suetsugu S.   +8 more
europepmc   +4 more sources

Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation [PDF]

Proceedings of the National Academy of Sciences, 2010
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, Ma, Qingjun, Vahedi-Faridi, Ardeschir, Sundborger, Anna, Pechstein, Arndt, Puchkov, Dmytro, Luo, Lin, Shupliakov, Oleg, Saenger, Wolfram, Haucke, Volker   +9 more
openaire   +6 more sources

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

Cell, 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   +3 more sources

The F-BAR domain of SRGP-1 facilitates cell-cell adhesion during C. elegans morphogenesis. [PDF]

J Cell Biol, 2010
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, Joyce MJ, Lynch AM, Witte K, Audhya A, Hardin J.   +5 more
europepmc   +5 more sources

Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation. [PDF]

Proc Natl Acad Sci U S A, 2012
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, Xue J, Wielens J, Smillie KJ, Anggono V, Parker MW, Cousin MA, Graham ME, Robinson PJ.   +8 more
europepmc   +10 more sources

The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially regulate membrane deformation [PDF]

Journal of Cell Science, 2012
Coordination of membrane deformation and cytoskeletal dynamics lies at the heart of many biological processes critical for cell polarity, motility and morphogenesis. We recently showed that slit-robo GTPase-activating protein 2 (srGAP2) regulates neuronal morphogenesis through the ability of its F-BAR domain to regulate membrane deformation and induce ...
Jaeda, Coutinho-Budd, Vladimir, Ghukasyan, Mark J, Zylka, Franck, Polleux   +3 more
openaire   +4 more sources

The F-BAR Domain of srGAP2 Induces Membrane Protrusions Required for Neuronal Migration and Morphogenesis [PDF]

Cell, 2009
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, Coutinho-Budd, Jaeda, Sassa, Takayuki, Gresset, Aurélie, Jordan, Nicole Vincent, Chen, Keng, Jin, Wei-Lin, Frost, Adam, Polleux, Franck   +8 more
openaire   +4 more sources

Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7

Nature Communications, 2019
The Bin/Amphiphysin/Rvs167 (BAR) domain superfamily, which includes FCH-BAR (F-BAR) domain proteins are membrane-sculpting proteins. Here the authors combine a range of techniques and show that the F-BAR domain of growth-arrest specific protein 7 (GAS7 ...
Kyoko Hanawa-Suetsugu, Yuzuru Itoh, Maisarah Ab Fatah, Tamako Nishimura, Kazuhiro Takemura, Kohei Takeshita, Satoru Kubota, Naoyuki Miyazaki, Wan Nurul Izzati Wan Mohamad Noor, Takehiko Inaba, Nhung Thi Hong Nguyen, Sayaka Hamada-Nakahara, Kayoko Oono-Yakura, Masashi Tachikawa, Kenji Iwasaki, Daisuke Kohda, Masaki Yamamoto, Akio Kitao, Atsushi Shimada, Shiro Suetsugu   +19 more
doaj   +2 more sources

The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis [PDF]

Cell Reports, 2016
F-BAR proteins link cellular membranes to the actin cytoskeleton in many biological processes. Here we investigated the function of the Schizosaccharomyces pombe Imp2 F-BAR domain in cytokinesis and find that it is critical for Imp2’s role in contractile
Nathan A. McDonald, Yoshimasa Takizawa, Anna Feoktistova, Ping Xu, Melanie D. Ohi, Craig W. Vander Kooi, Kathleen L. Gould   +6 more
doaj   +2 more sources

The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration [PDF]

Journal of Cell Science, 2011
The Rac1 GTPase controls cytoskeletal dynamics and is a key regulator of cell spreading and migration mediated by signaling through effector proteins, such as the PAK kinases and the Scar and WAVE proteins. We previously identified a series of regulatory proteins that associate with Rac1 through its hypervariable C-terminal domain, including the Rac1 ...
Kreu, B.J. de, Nethe, M., Fernandez-Borja, M., Anthony, E.C., Hensbergen, P.J., Deelder, A.M., Plomann, M., Hordijk, P.L.   +7 more
openaire   +6 more sources