Theoretical Study of the Effect of Ionospheric Return Currents on the Electron Temperature

An electron heat flow can occur in a partially ionized plasma in response to either an electron temperature gradient (thermal conduction) or an electron current (thermoelectric heat flow). The former process has been extensively studied, while the latter process has received relatively little attention. Therefore a time-dependent three-dimensional model of the high-latitude ionosphere was used to study the effect of field-aligned ionospheric return currents on auroral electron temperatures for different seasonal and solar cycle conditions as well as for different upper boundary heat fluxes. The results of this study lead to the following conclusions: (1) The average, large-scale, return current densities, which are a few microamps per square meter, are too small to affect auroral electron temperatures. (2) Current densities greater than about 10−5 A m−2 are needed for thermoelectric heat flow to be important. (3) The thermoelectric effect displays a marked solar cycle and seasonal dependence. (4) Thermoelectric heat transport corresponds to an upward flow of electron energy. (5) This energy flow can be either a source or sink of electron energy, depending on the altitude and geophysical conditions. (6) Thermoelectric heat transport is typically a sink above 300 km and acts to lower ambient electron temperatures by as much as 2000 K for field-aligned return current densities of the order of 5 × 10−5 A m−2. For this case, the electron temperature decreases with altitude above 300 km with a gradient that can exceed 1 K km−1. Also, the electron temperature can drop below both the ion and neutral temperatures in the upper F region owing to thermoelectric cooling. (7) A downward magnetospheric heat flux in combinations with an upward thermoelectric heat flux can produce steep positive electron temperature gradients in the topside ionosphere

A statistical study of the inner edge of the electron plasma sheet and the net convection potential as a function of geomagnetic activity

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/94691/1/jgra21076.pd

A model‐derived storm time asymmetric ring current driven electric field description

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/95674/1/jgra16075.pd

Integration of electrostatic and fluid dynamics within a dust devil

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/94610/1/jgre2050.pd

Inefficient Quality Control of Thermosensitive Proteins on the Plasma Membrane

BACKGROUND: Misfolded proteins are generally recognised by cellular quality control machinery, which typically results in their ubiquitination and degradation. For soluble cytoplasmic proteins, degradation is mediated by the proteasome. Membrane proteins that fail to fold correctly are subject to ER associated degradation (ERAD), which involves their extraction from the membrane and subsequent proteasome-dependent destruction. Proteins with abnormal transmembrane domains can also be recognised in the Golgi or endosomal system and targeted for destruction in the vacuole/lysosome. It is much less clear what happens to membrane proteins that reach their destination, such as the cell surface, and then suffer damage. METHODOLOGY/PRINCIPAL FINDINGS: We have tested the ability of yeast cells to degrade membrane proteins to which temperature-sensitive cytoplasmic alleles of the Ura3 protein or of phage lambda repressor have been fused. In soluble form, these proteins are rapidly degraded upon temperature shift, in part due to the action of the Doa10 and San1 ubiquitin ligases and the proteasome. When tethered to the ER protein Use1, they are also degraded. However, when tethered to a plasma membrane protein such as Sso1 they escape degradation, either in the vacuole or by the proteasome. CONCLUSIONS/SIGNIFICANCE: Membrane proteins with a misfolded cytoplasmic domain appear not to be efficiently recognised and degraded once they have escaped the ER, even though their defective domains are exposed to the cytoplasm and potentially to cytoplasmic quality controls. Membrane tethering may provide a way to reduce degradation of unstable proteins