Phosphatidylinositol 4,5-Bisphosphate (PtdIns(4,5)P2) Specifically Induces Membrane Penetration and Deformation by Bin/Amphiphysin/Rvs (BAR) Domains

Yoon, Yonghan; Zhang, Xiuqi; Cho, Wonhwa

doi:10.1074/jbc.m112.372789

Cited by 45 publications

(52 citation statements)

References 71 publications

(92 reference statements)

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“…In particular, this model attributes a role in vesicle fission to a preference of BAR domain proteins for PI(4,5)P 2 over PI(4)P. This affinity difference has been supported by equilibrium lipid binding studies for endophilin (13,28). We found a marked influence of phosphoinositides on kinetics, although revealing no significant difference comparing PI(4,5)P 2 and PI(4)P in association or dissociation (Fig.…”

Section: Role Of Electrostatics In the Association Phase Of The Mechamentioning

confidence: 47%

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Kinetics of Endophilin N-BAR Domain Dimerization and Membrane Interactions

Capraro

Shi

Wang

et al. 2013

Journal of Biological Chemistry

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Background: Endocytosis can involve dimerization and membrane association of the protein endophilin. Results: We found subnanomolar affinity for endophilin N-BAR dimerization. Membrane dissociation is substantially slower than association, and membrane-bound protein density-dependent. Conclusion: Endophilin binds membranes as dimers that subsequently oligomerize. Significance: Our findings illuminate the membrane binding mechanism of endophilin, which is important in understanding the regulation of membrane trafficking events.

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Section: Role Of Electrostatics In the Association Phase Of The Mechamentioning

confidence: 47%

“…However, beyond qualitative kinetic characterization by surface plasmon resonance (SPR) (28), little is known about the timescales and mechanisms determining the kinetics of endophilin-membrane interactions.…”

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confidence: 99%

Kinetics of Endophilin N-BAR Domain Dimerization and Membrane Interactions

Capraro

Shi

Wang

et al. 2013

Journal of Biological Chemistry

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“…The unique intracellular targeting of each member allows for the spatial and temporal control of the synthesis of PI(4,5)P 2 , thereby regulating specific processes, such as endocytosis, actin assembly, formation of cell-cell contacts and adhesion to the extracellular matrix Heck et al, 2007;Ling et al, 2006;Schill and Anderson, 2009a). PI(4,5)P 2 influences physiological processes by binding to proteins containing domains such as the pleckstrin-homology (PH) domain, phox-homology (PX) domain, band 4.1 ezrin radixin moesin homology (FERM) domain or the Bin/ Amphiphysin/Rvs (BAR) domain to modulate their activities (Betson et al, 2002;Harlan et al, 1994;Lemmon et al, 2002;Toker, 2002;Yoon et al, 2012). In particular, PI(4,5)P 2 regulates various components of the endocytic and endosomal trafficking pathways, including epsin, AP180, dynamin, sorting nexins (SNXs), ARFs and clathrin adaptor protein complexes Martin, 2001;Schill and Anderson, 2009a;Seet and Hong, 2006).…”

Section: Introductionmentioning

confidence: 99%

PIPKIγi5 regulates the endosomal trafficking and degradation of E-cadherin

Schill

Hedman

Choi

et al. 2014

Journal of Cell Science

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BSTRACTPhosphatidylinositol phosphate kinases (PIPKs) have distinct cellular targeting, allowing for site-specific synthesis of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P 2 ] to activate specific signaling cascades required for cellular processes. Several C-terminal splice variants of PIPKIc (also known as PIP5K1C) exist, and have been implicated in a multitude of cellular roles. PI(4,5)P 2 serves as a fundamental regulator of E-cadherin transport, and PI(4,5)P 2 -generating enzymes are important signaling relays in these pathways. We present evidence that the isoform 5 splice variant of PIPKIc (PIPKIci5) associates with E-cadherin and promotes its lysosomal degradation. Additionally, we show that the endosomal trafficking proteins SNX5 and SNX6 associate with PIPKIci5 and inhibit PIPKIci5-mediated Ecadherin degradation. Following HGF stimulation, activated Src directly phosphorylates PIPKIci5. Phosphorylation of the PIPKIci5 Cterminus regulates its association with SNX5 and, consequently, Ecadherin degradation. Additionally, this PIPKIci5-mediated pathway requires Rab7 to promote degradation of internalized E-cadherin. Taken together, the data indicate that PIPKIci5 and SNX5 are crucial regulators of E-cadherin sorting and degradation. PIPKIci5, SNX and phosphoinositide regulation of lysosomal sorting represent a novel area of PI(4,5)P 2 signaling and research. PIPKIci5 regulation of E-cadherin sorting for degradation might have broad implications in development and tissue maintenance, and enhanced PIPKIci5 function might have pathogenic consequences due to downregulation of E-cadherin.

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“…Furthermore, I-BAR proteins were observed to concentrate on constrictions of phagocytic cups, indicating their role in phagocytic uptake of pathogens [15]. Recent studies have reported a strong influence of PI(4,5)P 2 in the membrane deforming activity of BAR domain proteins [16].…”

Section: Membrane Curvature and Sorting At The Plasma Membranementioning

confidence: 96%

Plasma membrane reorganization: A glycolipid gateway for microbes

Aigal

Claudinon

Römer

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Ligand-receptor interactions, which represent the core for cell signaling and internalization processes are largely affected by the spatial configuration of host cell receptors. There is a growing piece of evidence that receptors are not homogeneously distributed within the plasma membrane, but are rather pre-clustered in nanodomains, or clusters are formed upon ligand binding. Pathogens have evolved many strategies to evade the host immune system and to ensure their survival by hijacking plasma membrane receptors that are most often associated with lipid rafts. In this review, we discuss the early stage molecular and physiological events that occur following ligand binding to host cell glycolipids. The ability of various biological ligands (e.g. toxins, lectins, viruses or bacteria) that bind to glycolipids to induce their own uptake into mammalian cells by creating negative membrane curvature and membrane invaginations is explored. We highlight recent trends in understanding nanoscale plasma membrane (re-)organization and present the benefits of using synthetic membrane systems. This article is part of a Special Issue entitled: Nanoscale membrane organisation and signalling.

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Phosphatidylinositol 4,5-Bisphosphate (PtdIns(4,5)P2) Specifically Induces Membrane Penetration and Deformation by Bin/Amphiphysin/Rvs (BAR) Domains

Cited by 45 publications

References 71 publications

Kinetics of Endophilin N-BAR Domain Dimerization and Membrane Interactions

Kinetics of Endophilin N-BAR Domain Dimerization and Membrane Interactions

PIPKIγi5 regulates the endosomal trafficking and degradation of E-cadherin

Plasma membrane reorganization: A glycolipid gateway for microbes

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