The BAR Domain Superfamily: Membrane-Molding Macromolecules

Frost, Adam; Unger, Vinzenz M.; Camilli, Pietro De

doi:10.1016/j.cell.2009.04.010

Cited by 540 publications

(573 citation statements)

References 44 publications

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“…Since SH3P2 contains a BAR domain ( Figure 1A), which is a wellknown membrane-binding module for membrane deformation (Frost et al, 2009), we propose that SH3P2 binds to the autophagosome membrane by itself to facilitate the expansion or fusion of autophagosome. Therefore, we next performed an in vitro liposome binding assay to test its membrane-binding capability.…”

Section: Sh3p2 Binds To Pi3p and Coordinates With The Pi3k Complex Tomentioning

confidence: 99%

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

et al. 2013

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Autophagy is a well-defined catabolic mechanism whereby cytoplasmic materials are engulfed into a structure termed the autophagosome. In plants, little is known about the underlying mechanism of autophagosome formation. In this study, we report that SH3 DOMAIN-CONTAINING PROTEIN2 (SH3P2), a Bin-Amphiphysin-Rvs domain-containing protein, translocates to the phagophore assembly site/preautophagosome structure (PAS) upon autophagy induction and actively participates in the membrane deformation process. Using the SH3P2-green fluorescent protein fusion as a reporter, we found that the PAS develops from a cup-shaped isolation membranes or endoplasmic reticulum-derived omegasome-like structures. Using an inducible RNA interference (RNAi) approach, we show that RNAi knockdown of SH3P2 is developmentally lethal and significantly suppresses autophagosome formation. An in vitro membrane/lipid binding assay demonstrates that SH3P2 is a membrane-associated protein that binds to phosphatidylinositol 3-phosphate. SH3P2 may facilitate membrane expansion or maturation in coordination with the phosphatidylinositol 3-kinase (PI3K) complex during autophagy, as SH3P2 promotes PI3K foci formation, while PI3K inhibitor treatment inhibits SH3P2 from translocating to autophagosomes. Further interaction analysis shows that SH3P2 associates with the PI3K complex and interacts with ATG8s in Arabidopsis thaliana, whereby SH3P2 may mediate autophagy. Thus, our study has identified SH3P2 as a novel regulator of autophagy and provided a conserved model for autophagosome biogenesis in Arabidopsis.

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Section: Sh3p2 Binds To Pi3p and Coordinates With The Pi3k Complex Tomentioning

confidence: 99%

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

et al. 2013

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“…The BAR domain is an elongated bundle of three curved a-helices (Peter et al 2004). Subgroups, with specific features of the BAR-domain modules, bear the designations N-BAR, F-BAR, and I-BAR (Frost et al 2009;Mim and Unger 2012). Homodimerization generates a symmetrical, usually arc-like molecule (that of FCHo1 is shown in Fig.…”

Section: Bar-domain Proteinsmentioning

confidence: 99%

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic

Kirchhausen

Owen

Harrison

2014

Cold Spring Harbor Perspectives in Biology

434

442

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Clathrin is a molecular scaffold for vesicular uptake of cargo at the plasma membrane, where its assembly into cage-like lattices underlies the clathrin-coated pits of classical endocytosis. This review describes the structures of clathrin, major cargo adaptors, and other proteins that participate in forming a clathrin-coated pit, loading its contents, pinching off the membrane as a lattice-enclosed vesicle, and recycling the components. It integrates as much of the structural information as possible at the time of writing into a sketch of the principal steps in coated-pit and coated-vesicle formation.

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“…Thus, based on the BAR domain shape of BIN1 and its general function as a membrane curvature protein, BIN1 has been referred to as the "banana" molecule (Qualmann et al, 2011). BIN1 has been implicated in many cellular processes, such as inducing membrane invagination (Frost et al, 2009) and initiating tubulogenesis in skeletal muscle cells (Lee et al, 2002). In human and mouse heart cells, BIN1 localizes to cardiac t-tubules (Hong et al, 2010), forms t-tubule membrane microdomains (Hong et al, 2014;Fu et al, 2016), facilitates cytoskeleton-based calcium channel trafficking to t-tubule membrane (Hong et al, 2010), and causes RyR movement along the SR membrane (Fu et al, 2016).…”

Section: Bin1 and Its Different Isoformsmentioning

confidence: 99%

Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health

Zhou

Hong

2016

Sci. China Life Sci.

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In recent decades, a cardiomyocyte membrane scaffolding protein bridging integrator 1 (BIN1) has emerged as a critical multifunctional regulator of transverse-tubule (t-tubule) function and calcium signaling in cardiomyocytes. Encoded by a single gene with 20 exons that are alternatively spliced, more than ten BIN1 protein isoforms are expressed with tissue and disease specificity. The recently discovered cardiac alternatively spliced isoform BIN1 (cBIN1 or BIN1+13+17)plays a crucial role in organizing membrane microfolds within cardiac t-tubules. These cBIN1-induced microfolds form functional dyad microdomains by trafficking L-type calcium channels (LTCC) to t-tubule membrane and recruiting ryanodine receptors (RyR) to junctional sarcoplasmic reticulum membrane. When cBIN1 is transcriptionally reduced as occurs in heart failure, cBIN1-microfolds are disrupted and fail to form LTCC and RyR couplons. As a result, impaired dyad formation limits excitation-contraction coupling thus cardiac contractility, and accumulation of orphaned leaky RyRs outside of dyads increases ventricular arrhythmias. Reduced myocardial BIN1 in heart failure is also detectable at the blood level, and plasma BIN1 level predicts heart failure progression and future arrhythmias in cardiomyopathy patients. Here we will review the recent progress in BIN1-related cardiomyocyte biology studies and discuss the diagnostic and predictive values of cBIN1 in future clinical use. heart failure, cBIN1, t-tubules, calcium transient, arrhythmias Citation:Zhou, K., and Hong, T. (2017). Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health.

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The BAR Domain Superfamily: Membrane-Molding Macromolecules

Cited by 540 publications

References 44 publications

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

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

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic

Cardiac BIN1 (cBIN1) is a regulator of cardiac contractile function and an emerging biomarker of heart muscle health

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