Results 11 to 20 of about 1,113,401 (243)

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, Bu W, Lee RT, Maurer-Stroh S, Goh WI.   +4 more
europepmc   +4 more sources

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   +3 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
SignificanceMembrane-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. Here we show that the neuronal membrane remodeling protein Nervous Wreck (Nwk) is autoinhibited by intramolecular ...
Stanishneva-Konovalova TB, Kelley CF, Eskin TL, Messelaar EM, Wasserman SA, Sokolova OS, Rodal AA.   +6 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, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA.   +6 more
europepmc   +4 more sources

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

Genes 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, Kazuaki, Umeda, Kazuya, Tsujita, Shiro, Suetsugu, Tadaomi, Takenawa, Hiroyuki, Nakanishi   +5 more
openaire   +3 more sources

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, Pluthero FG, Suphamungmee W, Giannini S, Christensen H, Leung R, Lo RW, Nakamura F, Lehman W, Plomann M, Hoffmeister KM, Kahr WH, Hartwig JH, Falet H.   +13 more
europepmc   +4 more sources

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
openaire   +2 more sources

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, Perera, Rushika, Roux, Aurélien, Spasov, Krasimir, Destaing, Olivier, Egelman, Edward H., De Camilli, Pietro, Unger, Vinzenz M.   +7 more
openaire   +2 more sources

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

iScience, 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, Yinyin Zhuang, Xinwen Miao, Yongpeng Zeng, Weibo Gao, Wenting Zhao, Min Wu   +6 more
doaj   +1 more source

“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   +2 more sources