Floating on the same plane: metropolis, money and the culture of abstraction

This article argues that the emergence of a trans-disciplinary discourse of ‘visual culture’ must be understood as, above all, a constitutively urban phenomenon. More specifically, it is in the historically new form of the capitalist metropolis, as described most famously by Simmel, that the ‘hyper-stimulus’ of modern visual culture has its social and spatial conditions. Paradoxically, however, it is as a result of this that visual culture studies is also intrinsically ‘haunted’ by a certain spectre of the invisible: one rooted in those forms of ‘real abstraction’ which Marx identifies with the commodity and the money form. Considering, initially, the canonical urban visual forms of the collage and the spectacle, these are each read in a certain relation to Simmel’s account of metropolitan life and of the money form, and, through this, to what the author claims are those forms of social and spatial abstraction that must be understood to animate them. Finally, the article returns to the entanglement of the visible and invisible entailed by this, and concludes by making some tentative suggestions about something like a paradoxical urban ‘aesthetic’ of abstraction on such a basis.

Aggregation Limits Surface Expression of Homomeric GluA3 Receptors

AMPA receptors are glutamate-gated cation channels assembled from GluA1-4 subunits and have properties that are strongly dependent on the subunit composition. The subunits have different propensities to form homomeric or various heteromeric receptors expressed on cell surface, but the underlying mechanisms are still poorly understood. Here, we examined the biochemical basis for the poor ability of GluA3 subunits to form homomeric receptors, linked previously to two amino acid residues, Y454 and R461, in its ligand-binding domain (LBD). Surface expression of GluA3 was improved by co-assembly with GluA2 but not with stargazin, a trafficking chaperone and modulator of AMPA receptors. The secretion efficiency of GluA2 and GluA3 LBDs paralleled the transport difference between the respective full-length receptors and was similarly dependent on Y454/R461, but not on LBD stability. In comparison to GluA2, GluA3 homomeric receptors showed a strong and Y454/R461-dependent tendency to aggregate both in the macroscopic scale measured as lower solubility in nonionic detergent and in the microscopic scale evident as the preponderance of hydrodynamically large structures in density gradient centrifugation and native gel electrophoresis. We conclude that the impaired surface expression of homomeric GluA3 receptors is caused by nonproductive assembly and aggregation to which LBD residues Y454 and R461 strongly contribute. This aggregation inhibits the entry of newly synthesized GluA3 receptors to the secretory pathway.