scholarly journals Comparing physical mechanisms for membrane curvature-driven sorting of BAR-domain proteins

Soft Matter ◽  
2021 ◽  
Vol 17 (16) ◽  
pp. 4254-4265
Author(s):  
Feng-Ching Tsai ◽  
Mijo Simunovic ◽  
Benoit Sorre ◽  
Aurélie Bertin ◽  
John Manzi ◽  
...  
Keyword(s):  
Theoretical Models ◽  
Membrane Curvature ◽  
Bar Domain ◽  
Curvature Sensing ◽  
Physical Mechanisms ◽  
Electron Microscopy Data ◽  
Bar Domain Proteins ◽  
Microscopy Data ◽  
Curvature Driven ◽  
Review Current

We review current theoretical models for curvature sensing of BAR-domain proteins, test the models on 2 proteins, and present new electron microscopy data on the organization of BAR domains on tubes.

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 Bar Domain Proteins can Differ Substantially in their Capacity to Generate Membrane Curvature

2016 ◽  
Vol 110 (3) ◽  
pp. 357a
Author(s):  
Zhiming Chen ◽  
Zheng Shi ◽  
Katarzyna I. Jankowska ◽  
Tobias Baumgart
Keyword(s):  
Membrane Curvature ◽  
Bar Domain ◽  
Bar Domain Proteins

scholarly journals Comparative study of curvature sensing mediated by F-BAR domain and an intrinsically disordered region of FBP17

2020 ◽  
Author(s):  
Maohan Su ◽  
Yinyin Zhuang ◽  
Xinwen Miao ◽  
Yongpeng Zeng ◽  
Weibo Gao ◽  
...  
Keyword(s):  
Lipid Bilayer ◽  
Membrane Trafficking ◽  
Membrane Curvature ◽  
Wave System ◽  
Common Belief ◽  
Bar Domain ◽  
Curvature Sensing ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Region

Membrane curvature has emerged as an intriguing physical organization principle underlying biological signaling and membrane trafficking. FBP17 of the CIP4/FBP17/Toca-1 F-BAR family is unique in the BAR family because its structurally folded F-BAR domain does not contain any hydrophobic motifs that insert into lipid bilayer. While it has been widely assumed so, whether the banana-shaped F-BAR domain alone can sense curvature has never been experimentally demonstrated. Using a nanopillar-supported lipid bilayer system, we found that the F-BAR domain of FBP17 displayed minimal curvature sensing in vitro. We further identified an alternatively spliced intrinsically disordered region (IDR) of FBP17 next to its F-BAR domain that is conserved in sequence across species. The IDR senses membrane curvature and its sensing ability greatly exceeds that of F-BAR domain alone. In living cells, presence of the IDR domain changed the dynamics of FBP17 recruitment in a curvature-coupled cortical wave system. Collectively, we propose that FBP17 does sense curvature but contrary to the common belief, its curvature sensing capability largely originates from its disordered region, not F-BAR domain itself.

scholarly journals Membrane curvature directs the localization of Cdc42p to novel foci required for cell–cell fusion

2017 ◽  
Vol 216 (12) ◽  
pp. 3971-3980 ◽  
Author(s):  
Jean A. Smith ◽  
Allison E. Hall ◽  
Mark D. Rose
Keyword(s):  
Cell Fusion ◽  
Fusion Proteins ◽  
Cell Walls ◽  
Rho Gtpase ◽  
Membrane Curvature ◽  
Cell Wall Degradation ◽  
Focus Formation ◽  
Mutant Analysis ◽  
Bar Domain ◽  
Bar Domain Proteins

Cell fusion is ubiquitous in eukaryotic fertilization and development. The highly conserved Rho–GTPase Cdc42p promotes yeast fusion through interaction with Fus2p, a pheromone-induced amphiphysin-like protein. We show that in prezygotes, Cdc42p forms a novel Fus2p-dependent focus at the center of the zone of cell fusion (ZCF) and remains associated with remnant cell walls after initial fusion. At the ZCF and during fusion, Cdc42p and Fus2p colocalized. In contrast, in shmoos, both proteins were near the cortex but spatially separate. Cdc42p focus formation depends on ZCF membrane curvature: mutant analysis showed that Cdc42p localization is negatively affected by shmoo-like positive ZCF curvature, consistent with the flattening of the ZCF during fusion. BAR-domain proteins such as the fusion proteins Fus2p and Rvs161p are known to recognize membrane curvature. We find that mutations that disrupt binding of the Fus2p/Rvs161p heterodimer to membranes affect Cdc42p ZCF localization. We propose that Fus2p localizes Cdc42p to the flat ZCF to promote cell wall degradation.

scholarly journals Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis

2010 ◽  
Vol 21 (17) ◽  
pp. 3054-3069 ◽  
Author(s):  
Ji-Young Youn ◽  
Helena Friesen ◽  
Takuma Kishimoto ◽  
William M. Henne ◽  
Christoph F. Kurat ◽  
...  
Keyword(s):  
Membrane Binding ◽  
Membrane Curvature ◽  
Cortical Actin ◽  
Independent Manner ◽  
Yeast Saccharomyces Cerevisiae ◽  
Tubule Formation ◽  
Bar Domain ◽  
Bar Domain Proteins ◽  
Bar Domains

BAR domains are protein modules that bind to membranes and promote membrane curvature. One type of BAR domain, the N-BAR domain, contains an additional N-terminal amphipathic helix, which contributes to membrane-binding and bending activities. The only known N-BAR-domain proteins in the budding yeast Saccharomyces cerevisiae, Rvs161 and Rvs167, are required for endocytosis. We have explored the mechanism of N-BAR-domain function in the endocytosis process using a combined biochemical and genetic approach. We show that the purified Rvs161–Rvs167 complex binds to liposomes in a curvature-independent manner and promotes tubule formation in vitro. Consistent with the known role of BAR domain polymerization in membrane bending, we found that Rvs167 BAR domains interact with each other at cortical actin patches in vivo. To characterize N-BAR-domain function in endocytosis, we constructed yeast strains harboring changes in conserved residues in the Rvs161 and Rvs167 N-BAR domains. In vivo analysis of the rvs endocytosis mutants suggests that Rvs proteins are initially recruited to sites of endocytosis through their membrane-binding ability. We show that inappropriate regulation of complex sphingolipid and phosphoinositide levels in the membrane can impinge on Rvs function, highlighting the relationship between membrane components and N-BAR-domain proteins in vivo.

scholarly journals External push and internal pull forces recruit curvature-sensing N-BAR domain proteins to the plasma membrane

2012 ◽  
Vol 14 (8) ◽  
pp. 874-881 ◽  
Author(s):  
Milos Galic ◽  
Sangmoo Jeong ◽  
Feng-Chiao Tsai ◽  
Lydia-Marie Joubert ◽  
Yi I. Wu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Bar Domain ◽  
Curvature Sensing ◽  
Bar Domain Proteins

scholarly journals Dynamic recruitment of the curvature-sensitive protein ArhGAP44 to nanoscale membrane deformations limits exploratory filopodia initiation in neurons

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Milos Galic ◽  
Feng-Chiao Tsai ◽  
Sean R Collins ◽  
Maja Matis ◽  
Samuel Bandara ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Neuronal Development ◽  
Membrane Curvature ◽  
Gtp Hydrolysis ◽  
Bar Domain ◽  
Curvature Sensing ◽  
Contractile Forces ◽  
Dendritic Branches ◽  
Membrane Deformations ◽  
Protein Recruitment

In the vertebrate central nervous system, exploratory filopodia transiently form on dendritic branches to sample the neuronal environment and initiate new trans-neuronal contacts. While much is known about the molecules that control filopodia extension and subsequent maturation into functional synapses, the mechanisms that regulate initiation of these dynamic, actin-rich structures have remained elusive. Here, we find that filopodia initiation is suppressed by recruitment of ArhGAP44 to actin-patches that seed filopodia. Recruitment is mediated by binding of a membrane curvature-sensing ArhGAP44 N-BAR domain to plasma membrane sections that were deformed inward by acto-myosin mediated contractile forces. A GAP domain in ArhGAP44 triggers local Rac-GTP hydrolysis, thus reducing actin polymerization required for filopodia formation. Additionally, ArhGAP44 expression increases during neuronal development, concurrent with a decrease in the rate of filopodia formation. Together, our data reveals a local auto-regulatory mechanism that limits initiation of filopodia via protein recruitment to nanoscale membrane deformations.

scholarly journals The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

2006 ◽  
Vol 70 (1) ◽  
pp. 37-120 ◽  
Author(s):  
Gang Ren ◽  
Parimala Vajjhala ◽  
Janet S. Lee ◽  
Barbara Winsor ◽  
Alan L. Munn
Keyword(s):  
Transcriptional Repression ◽  
Three Dimensional ◽  
Coiled Coil ◽  
Helical Structure ◽  
Secretory Vesicle ◽  
Membrane Curvature ◽  
Dimensional Structure ◽  
Valuable Insight ◽  
Bar Domain ◽  
Bar Domain Proteins

SUMMARY The Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.

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