scholarly journals Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures

2011 ◽  
Vol 18 (8) ◽  
pp. 902-907 ◽  
Author(s):  
Anette Pykäläinen ◽  
Malgorzata Boczkowska ◽  
Hongxia Zhao ◽  
Juha Saarikangas ◽  
Grzegorz Rebowski ◽  
...  
Keyword(s):  
Membrane Structures ◽  
Bar Domain ◽  
Domain Protein ◽  
Planar Membrane

Dynamin 2 and BAR domain protein pacsin 2 cooperatively regulate formation and maturation of podosomes

2021 ◽  
Vol 571 ◽  
pp. 145-151
Author(s):  
Jianzhen Li ◽  
Kenshiro Fujise ◽  
Haymar Wint ◽  
Yosuke Senju ◽  
Shiro Suetsugu ◽  
...  
Keyword(s):  
Bar Domain ◽  
Domain Protein ◽  
Dynamin 2

scholarly journals FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure and function

2018 ◽  
Vol 218 (1) ◽  
pp. 97-111 ◽  
Author(s):  
Liang Wang ◽  
Ziyi Yan ◽  
Helena Vihinen ◽  
Ove Eriksson ◽  
Weihuan Wang ◽  
...  
Keyword(s):  
Mitochondrial Function ◽  
Molecular Mechanisms ◽  
Membrane Curvature ◽  
Mitochondrial Morphology ◽  
Membrane Remodeling ◽  
Mitochondrial Ultrastructure ◽  
Bar Domain ◽  
Bar Domain Proteins ◽  
Domain Protein

Mitochondrial function is closely linked to its dynamic membrane ultrastructure. The mitochondrial inner membrane (MIM) can form extensive membrane invaginations known as cristae, which contain the respiratory chain and ATP synthase for oxidative phosphorylation. The molecular mechanisms regulating mitochondrial ultrastructure remain poorly understood. The Bin-Amphiphysin-Rvs (BAR) domain proteins are central regulators of diverse cellular processes related to membrane remodeling and dynamics. Whether BAR domain proteins are involved in sculpting membranes in specific submitochondrial compartments is largely unknown. In this study, we report FAM92A1 as a novel BAR domain protein localizes to the matrix side of the MIM. Loss of FAM92A1 caused a severe disruption to mitochondrial morphology and ultrastructure, impairing organelle bioenergetics. Furthermore, FAM92A1 displayed a membrane-remodeling activity in vitro, inducing a high degree of membrane curvature. Collectively, our findings uncover a role for a BAR domain protein as a critical organizer of the mitochondrial ultrastructure that is indispensable for mitochondrial function.

scholarly journals The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration

2011 ◽  
Vol 124 (14) ◽  
pp. 2375-2388 ◽  
Author(s):  
B.-J. de Kreuk ◽  
M. Nethe ◽  
M. Fernandez-Borja ◽  
E. C. Anthony ◽  
P. J. Hensbergen ◽  
...  
Keyword(s):  
Cell Spreading ◽  
Bar Domain ◽  
Domain Protein ◽  
And Migration

scholarly journals A BAR-Domain Protein SH3P2, Which Binds to Phosphatidylinositol 3-Phosphate and ATG8, Regulates Autophagosome Formation in Arabidopsis

2013 ◽  
Vol 25 (11) ◽  
pp. 4596-4615 ◽  
Author(s):  
X. Zhuang ◽  
H. Wang ◽  
S. K. Lam ◽  
C. Gao ◽  
X. Wang ◽  
...  
Keyword(s):  
Autophagosome Formation ◽  
Bar Domain ◽  
Domain Protein ◽  
Phosphatidylinositol 3

P.776 Targeting of an F-BAR domain protein to the synaptic periactive zone ensures uniform size of synaptic vesicles

2020 ◽  
Vol 40 ◽  
pp. S440-S441
Author(s):  
O. Shupliakov ◽  
N. Akkuratova ◽  
O. Korenkova ◽  
K. Onohin ◽  
E. Sopova ◽  
...  
Keyword(s):  
Synaptic Vesicles ◽  
Uniform Size ◽  
Bar Domain ◽  
Domain Protein

scholarly journals F-BAR domain protein Syndapin regulates actomyosin dynamics during apical cap remodeling in syncytial Drosophila embryos

2020 ◽  
Vol 133 (10) ◽  
pp. jcs235846
Author(s):  
Aparna Sherlekar ◽  
Gayatri Mundhe ◽  
Prachi Richa ◽  
Bipasha Dey ◽  
Swati Sharma ◽  
...  
Keyword(s):  
Bar Domain ◽  
Domain Protein ◽  
Drosophila Embryos

scholarly journals Syndapin Promotes Formation of a Postsynaptic Membrane System in Drosophila

2009 ◽  
Vol 20 (8) ◽  
pp. 2254-2264 ◽  
Author(s):  
Vimlesh Kumar ◽  
Robert Fricke ◽  
Debjani Bhar ◽  
Suneel Reddy-Alla ◽  
K. S. Krishnan ◽  
...  
Keyword(s):  
Protein Function ◽  
Cultured Cells ◽  
Neuromuscular Junctions ◽  
Membrane System ◽  
Postsynaptic Membrane ◽  
Membrane Structures ◽  
Bar Domain ◽  
Membrane Tubulation

Syndapins belong to the F-BAR domain protein family whose predicted functions in membrane tubulation remain poorly studied in vivo. At Drosophila neuromuscular junctions, syndapin is associated predominantly with a tubulolamellar postsynaptic membrane system known as the subsynaptic reticulum (SSR). We show that syndapin overexpression greatly expands this postsynaptic membrane system. Syndapin can expand the SSR in the absence of dPAK and Dlg, two known regulators of SSR development. Syndapin's N-terminal F-BAR domain, required for membrane tubulation in cultured cells, is required for SSR expansion. Consistent with a model in which syndapin acts directly on postsynaptic membrane, SSR expansion requires conserved residues essential for membrane binding in vitro. However, syndapin's Src homology (SH) 3 domain, which negatively regulates membrane tubulation in cultured cells, is required for synaptic targeting and strong SSR induction. Our observations advance knowledge of syndapin protein function by 1) demonstrating the in vivo relevance of membrane remodeling mechanisms suggested by previous in vitro and structural analyses, 2) showing that SH3 domains are necessary for membrane expansion observed in vivo, and 3) confirming that F-BAR proteins control complex membrane structures.

Stiffness Characteristics of Membrane Space Structures Supported by Booms

2012 ◽  
Author(s):  
H. Tamaru ◽  
T. Akita ◽  
M. C. Natori ◽  
H. Yamakawa
Keyword(s):  
Finite Element ◽  
Parametric Study ◽  
Vibration Characteristics ◽  
Space Structures ◽  
Finite Element Code ◽  
Membrane Structures ◽  
Square Planar ◽  
Applied Tension ◽  
Planar Membrane ◽  
Stiffness Characteristics

A systematic parametric study on the stiffness characteristics of compound space structures consisted of membranes and booms is presented. Using a tension field finite element code including membrane wrinkle effects, basic vibration characteristics of a square planar membrane structures are shown, and the effects of various conditions of applied tension between membrane and boom elements are discussed.

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