Magnetic Catalysis and Quantum Hall Ferromagnetism in Weakly Coupled Graphene

We study the realization in a model of graphene of the phenomenon whereby the tendency of gauge-field mediated interactions to break chiral symmetry spontaneously is greatly enhanced in an external magnetic field. We prove that, in the weak coupling limit, and where the electron-electron interaction satisfies certain mild conditions, the ground state of charge neutral graphene in an external magnetic field is a quantum Hall ferromagnet which spontaneously breaks the emergent U(4) symmetry to U(2)XU(2). We argue that, due to a residual CP symmetry, the quantum Hall ferromagnet order parameter is given exactly by the leading order in perturbation theory. On the other hand, the chiral condensate which is the order parameter for chiral symmetry breaking generically obtains contributions at all orders. We compute the leading correction to the chiral condensate. We argue that the ensuing fermion spectrum resembles that of massive fermions with a vanishing U(4)-valued chemical potential. We discuss the realization of parity and charge conjugation symmetries and argue that, in the context of our model, the charge neutral quantum Hall state in graphene is a bulk insulator, with vanishing longitudinal conductivity due to a charge gap and Hall conductivity vanishing due to a residual discrete particle-hole symmetry.Comment: 35 page

Niclosamide Prevents the Formation of Large Ubiquitin-Containing Aggregates Caused by Proteasome Inhibition

Protein aggregation is a hallmark of many neurodegenerative diseases and has been linked to the failure to degrade misfolded and damaged proteins. In the cell, aberrant proteins are degraded by the ubiquitin proteasome system that mainly targets short-lived proteins, or by the lysosomes that mostly clear long-lived and poorly soluble proteins. Both systems are interconnected and, in some instances, autophagy can redirect proteasome substrates to the lysosomes.To better understand the interplay between these two systems, we established a neuroblastoma cell population stably expressing the GFP-ubiquitin fusion protein. We show that inhibition of the proteasome leads to the formation of large ubiquitin-containing inclusions accompanied by lower solubility of the ubiquitin conjugates. Strikingly, the formation of the ubiquitin-containing aggregates does not require ectopic expression of disease-specific proteins. Moreover, formation of these focused inclusions caused by proteasome inhibition requires the lysine 63 (K63) of ubiquitin. We then assessed selected compounds that stimulate autophagy and found that the antihelmintic chemical niclosamide prevents large aggregate formation induced by proteasome inhibition, while the prototypical mTORC1 inhibitor rapamycin had no apparent effect. Niclosamide also precludes the accumulation of poly-ubiquitinated proteins and of p62 upon proteasome inhibition. Moreover, niclosamide induces a change in lysosome distribution in the cell that, in the absence of proteasome activity, may favor the uptake into lysosomes of ubiquitinated proteins before they form large aggregates.Our results indicate that proteasome inhibition provokes the formation of large ubiquitin containing aggregates in tissue culture cells, even in the absence of disease specific proteins. Furthermore our study suggests that the autophagy-inducing compound niclosamide may promote the selective clearance of ubiquitinated proteins in the absence of proteasome activity