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Electric and magnetic fields have been used in various ways to enhance the performance of lubrication systems. The presence of these fields can significantly change the properties of lubricants. The rapid adoption of electric vehicles (EVs) has presented newlubrication-related challenges due to the presence of electric current. There is an urgent need for an in-depth study of lubrication systems subjected to such fields. This paper highlights recent research works on several key areas of lubrication involving electric or magnetic fields, which are:1) electric double layer in lubrication, 2) electrorheological fluids, 3) magnetorheological fluids, 4) ferrofluids, and 5) typical fluids used in the current EVs and typical surface failures of bearing components in EVs. Commonly used lubricants in each area are reviewed; lubrication mechanisms and related mathematical models are summarized; methods for and results from numerical analyses and experimental explorations are discussed; and common features of lubrications in different fields are explored. Based on the current research progress in these fields and the classic generalized Reynolds equation, a generalized mechanical-electro-magnetic-thermal-field (MEMT-field) Reynolds equation is proposed to describe the aforementioned lubrication scenarios and the effects of coupled mechanical, electric, magnetic, and thermal fields, which can be solved with a numerical iteration method. [ABSTRACT FROM AUTHOR]

Previous work from our laboratory and others has established that Ste-20-related proline-alanine-rich kinase (SPAK/PASK) is central to the regulation of NKCC1 function. With no lysine (K) kinase (WNK4) has also been implicated in the regulation of NKCC1 activity through upstream activation of SPAK. Because previous studies from our laboratory also demonstrated a protein-protein interaction between SPAK and apoptosis-associated tyrosine kinase (AATYK), we explore here the possibility that AATYK is another component of the regulation of NKCC1. Heterologous expression of AATYK1 in NKCC1-injected Xenopus laevis oocytes markedly inhibited cotransporter activity under isosmotic conditions. Interestingly, mutation of key residues in the catalytic domain of AATYK1 revealed that the kinase activity does not play a role in the suppression of NKCC1 function. However, mutagenesis of the two SPAK-binding motifs in AATYK1 completely abrogated this effect. As protein phosphatase 1 (PP1) also plays a central role in the dephosphorylation and inactivation of NKCC1, we investigated the possibility that AATYK1 interacts with the phosphatase. We identified a PP1 docking motif in AATYK1 and demonstrated interaction using yeast-2-hybrid analysis. Mutation of a key valine residue (V1175) within this motif prevented protein-protein interaction. Furthermore, the physical interaction between PP1 and AATYK was required for inhibition of NKCC1 activity in Xenopus laevis oocytes. Taken together, our data are consistent with AATYK1 indirectly inhibiting the SPAK/WNK4 activation of the cotransporter by scaffolding an inhibitory phosphatase in proximity to a stimulatory kinase. ion fluxes; Xenopus laevis oocytes; yeast-2 hybrid; phosphorylation doi:10.1152/ajpcell.00580.2006

In the present study, we have demonstrated functional interaction between Ste20-related proline-alanine-rich kinase (SPAK), WNK4 [with no lysine (K)], and the widely expressed [Na.sup.+]-[K.sup.+]-2[C1.sup.-] cotransporter type 1 (NKCCI). NKCCI function, which we measured in Xenopus laevis oocytes under both isosmotic (basal) and hyperosmotic (stimulated) conditions, was unaffected when SPAK and WNK4 were expressed alone. In contrast, expression of both kinases with NKCC1 resulted in a significant increase in cotransporter activity and an insensitivity to external osmolarity or cell volume. NKCCI activation is dependent on the catalytic activity of SPAK and likely also of WNK4, because mutations in their catalytic domains result in an absence of cotransporter stimulation. The results of our yeast two-hybrid experiments suggest that WNK4 does not interact directly with NKCC 1 but does interact with SPAK. Functional experiments demonstrated that the binding of SPAK to WNK4 was also required because a SPAK-interaction-deficient WNK4 mutant (Phe997Ala) did not increase NKCC1 activity. We also have shown that the transport function of [K.sup.+]-[Cl.sup.-] cotransporter type 2 (KCC2), a neuron-specific KC1 cotransporter, was diminished by the expression of both kinases under both isosmotic and hyposmotic conditions. Our data are consistent with WNK4 interacting with SPAK, which in turn phosphorylates and activates NKCC1 and phosphorylates and deactivates KCC2. bumetanide; [Na.sup.+]-[K.sup.+]-2[C1.sup.-] cotransporter; [K.sup.+]-CI- cotransporter; Xenopus oocytes