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2002 ; . Further, Kv1.2 does not appear to interact with Src in this way, suggesting somewhat different mechanisms for Kv1.2 vs. Kv1.5 regulation. Kv1.3 is also regulated by tyrosine kinases, but a study examining the possible internalization of Kv1.3 as a mechanism of channel suppression yielded negative results Fadool et al., 1997 ; . However, that interpretation may have been limited by the methodological scope of the experiments themselves. Changes in the level of surface Kv1.3 were inferred from differential antibody labeling of surface vs. internal Kv1.3 followed by detection with indirect immunofluoresence. Quantification of that data was limited to a relatively small sample size and may therefore have been unable to detect small but significant changes in surface channel levels. In the studies presented here, changes in Kv1.2 surface expression were assayed using a variety of more sensitive techniques, including biochemical and flow cytometric studies capable of measuring surface Kv1.2 in thousands of cells per experiment. Using those methods, we find that tyrosine kinase-dependent modulation of Kv1.2 involves the regulated trafficking of the channel from the plasma membrane. This implies that tyrosine kinase-mediated endocytosis is a mechanism for effecting acute changes in membrane excitability associated with Kv1.2 suppression, including hyperexcitability associated with seizure in the cerebral cortex Lambe and Aghajanian, 2001 ; as well as changes in smooth muscle excitability associated with hypertension Kerr et al., 2001; Thorneloe et al., 2001; Lu et al., 2002 ; . The initial indication that the levels of Kv1.2 within the plasma membrane might be regulated by posttranslational modification came from the observation that surface Kv1.2 levels varied independently of the total Kv1.2 expressed within unstimulated cells Figure 1 ; . Surface expression of Kv1.2 can also be enhanced by the Kv 2 subunit, which influences Kv1.2 trafficking to the plasma membrane in some situations Shi et al., 1996; Trimmer, 1998 ; . However, because the Kv 2 subunit was stably expressed along with Kv1.2 in the cell line used in these studies, we surmised that another mechanism for differential Kv1.2 surface expression was at play, leading to the discovery that surface-expressed Kv1.2 undergoes stimulus-induced endocytosis. Thus, Kv1.2 surface expression is under two forms of regulatory control, one involving the Kv 2-dependent trafficking of newly synthesized channel to the plasma membrane and the other involving stimulus-induced trafficking of the channel from the plasma membrane through endocytosis. Whether the two processes are related is unclear. We note that Kv1.2 endocytosis does occur in hippocampal neurons transfected with Kv1.2 alone Figure 4 ; , suggesting that stoichiometric levels of Kv 2 may not be required for channel endocytosis in neurons. This parallels in vivo knockout studies suggesting that, in contrast to the case in heterologous expression systems Shi et al., 1996 ; , Kv 2 is not required for efficient maturation and trafficking of native Kv1.2 in neurons McCormack et al., 2002 ; . McCormack et al. 2002 ; suggest several plausible explanations for that difference, including the compensatory expression of functionally similar beta subunit isotypes, developmental dependency of Kv 2 effects, or a beta-subunit-independent mechanism for Kv1.2 trafficking to the plasma membrane in neurons. Regarding the latter possibility, McCormack et al. note that, in contrast to the exclusive expression of the Kv1.2-alpha subunit in a heterologous system, native expression of Kv1.2 is often accompanied by expression of other Kv1 alpha subunits, some of which may replace Kv 2 in effecting Kv1.2 trafficking to the cell surface Manganas and Trimmer, 2000 ; . Therefore, Kv 2 may be required to observe endocytosis in heterologous, because topical oxsoralen. From large-scale questions of how to make district and state-wide systems interoperate, to local questions of how media integrates with classroom tools such as powerpoint ; , the requirements of a single standard for digital delivery are massive and more complex than any standard for digital content currently present in the education or consumer market and metoclopramide.

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