Quantum Group as Semi-infinite Cohomology

We obtain the quantum group $SL_q(2)$ as semi-infinite cohomology of the Virasoro algebra with values in a tensor product of two braided vertex operator algebras with complementary central charges $c+\bar{c}=26$. Each braided VOA is constructed from the free Fock space realization of the Virasoro algebra with an additional q-deformed harmonic oscillator degree of freedom. The braided VOA structure arises from the theory of local systems over configuration spaces and it yields an associative algebra structure on the cohomology. We explicitly provide the four cohomology classes that serve as the generators of $SL_q(2)$ and verify their relations. We also discuss the possible extensions of our construction and its connection to the Liouville model and minimal string theory.Comment: 50 pages, 7 figures, minor revisions, typos corrected, Communications in Mathematical Physics, in pres

Nonpolarized Cells Selectively Sort Apical Proteins from Cell Surface to a Novel Compartment, but Lack Apical Retention Mechanisms

Membrane trafficking is central to establishing and maintaining epithelial cell polarity. One open question is to what extent the mechanisms regulating membrane trafficking are conserved between nonpolarized and polarized cells. To answer this question, we examined the dynamics of domain-specific plasma membrane (PM) proteins in three classes of hepatic cells: polarized and differentiated WIF-B cells, nonpolarized and differentiated Fao cells, and nonpolarized and nondifferentiated Clone 9 cells. In nonpolarized cells, mature apical proteins were uniformly distributed in the PM. Surprisingly, they were also in an intracellular compartment. Double labeling revealed that the compartment contained only apical proteins. By monitoring the dynamics of antibody-labeled molecules in nonpolarized cells, we further found that apical proteins rapidly recycled between the compartment and PM. In contrast, the apical PM residents in polarized cells showed neither internalization nor return to the basolateral PM from which they had originally come. Cytochalasin D treatment of these polarized cells revealed that the retention mechanisms are actin dependent. We conclude from these data that both polarized and nonpolarized cells selectively sort apical proteins from the PM and transport them to specific, but different cellular locations. We propose that the intracellular recycling compartment in nonpolarized cells is an intermediate in apical surface formation

Erratum: Large meta-analysis of genome-wide association studies identifies five loci for lean body mass.

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