The Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition

Casal, Eva; Federici, L.; Zhang, Wei; Fernández‐Recio, Juan; Priego, Eva-Marı́a; Miguel, Ricardo Núñez; DuHadaway, James B.; Prendergast, George C.; Luisi, Ben F.; Laue, Ernest D.

doi:10.1021/bi060717k

Cited by 70 publications

(75 citation statements)

References 44 publications

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“…CNT-1 harbors an N-terminal BAR domain. Proteins with BAR domains, such as amphiphysin, endophilins, and sorting nexins, have been reported to sense membrane curvature and to induce positive curvature, features that are important in membrane budding and tubulation (33). Recruited to the membrane by RAB-10, CNT-1 might be localized further to high-curvature regions of budding vesicles or tubules through its BAR domain or might help remodel functional subdomains or buds on endosomes, facilitating sequestration of recycling cargo.…”

Section: Discussionmentioning

confidence: 99%

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

Shi

Liu²,

Koenig

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

107

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Caenorhabditis elegans RAB-10 and mammalian Rab10 are key regulators of endocytic recycling, especially in the basolateral recycling pathways of polarized epithelial cells. To understand better how RAB-10 contributes to recycling endosome function, we sought to identify RAB-10 effectors. One RAB-10-binding partner that we identified, CNT-1, is the only C. elegans homolog of the mammalian Arf6 GTPase-activating proteins ACAP1 and ACAP2. Arf6 is known to regulate endosome-to-plasma membrane transport, in part through activation of type I phophatidylinositol-4-phosphate 5 kinase. Here we show that CNT-1 binds to RAB-10 through its C-terminal ankyrin repeats and colocalizes with RAB-10 and ARF-6 on recycling endosomes in vivo. Furthermore, we find that RAB-10 is required for the recruitment of CNT-1 to endosomal membranes in the intestinal epithelium. Consistent with negative regulation of ARF-6 by RAB-10 and CNT-1, we found overaccumulation of endosomal phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] in cnt-1 and rab-10 mutants and reduced endosomal PI(4,5)P2 levels in arf-6 mutants. These mutants produced similar effects on endosomal recruitment of the PI(4,5)P2-dependent membrane-bending proteins RME-1/Ehd and SDPN-1/Syndapin/Pacsin and resulted in endosomal trapping of specific recycling cargo. Our studies identify a RAB-10-to-ARF-6 regulatory loop required to regulate endosomal PI(4,5)P2, a key phosphoinositide in membrane traffic. membrane lipid | clathrin

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Section: Discussionmentioning

confidence: 99%

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

Shi

Liu²,

Koenig

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

107

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“…Thus the domain structure of these proteins (Toca-1, IRSp53, CIP4, and FBP17) could allow the coupling of the membrane curvature with actin dynamics under the control of Cdc42. Interestingly, structural and functional studies of the IRSp53 I-BAR domain suggest it would induce membrane curvature opposite that of proteins such as amphiphysin leading to membrane protrusion rather than membrane invagination (16,42) and hence the designation I (Inverse)-BAR domain. Here, we show that the IRSp53 I-BAR domain induces dynamic membrane protrusions that lack actin in live mammalian cells (see Fig.…”

Section: Discussionmentioning

confidence: 99%

The Cdc42 Effector IRSp53 Generates Filopodia by Coupling Membrane Protrusion with Actin Dynamics

Lim

Goh

et al. 2008

Journal of Biological Chemistry

147

225

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“…As a member of the BAR-domain containing protein superfamily, BIN1 contains a signature N-terminal BAR-domain (N-BAR) encoded by exons 1-9. The crystal structure of the N-BAR domain revealed a dimeric interaction between helixes from each monomer to form a 6-helix bundle in BIN1 dimers (Casal et al, 2006). The structure of this dimer is similar to an elongated banana shape (Peter et al, 2004;Fu and Hong, 2015).…”

Section: Bin1 and Its Different Isoformsmentioning

confidence: 94%

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 Crystal Structure of the BAR Domain from Human Bin1/Amphiphysin II and Its Implications for Molecular Recognition

Cited by 70 publications

References 44 publications

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

The Cdc42 Effector IRSp53 Generates Filopodia by Coupling Membrane Protrusion with Actin Dynamics

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

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