ausblenden:
Schlagwörter:
Alf1
Btx
Ca-CaM
CaMKII
Cav-1
Cholesterol
Cyclodextrin
Drm
Eag1
Flot-2
Gm1
Gm130
GalCer
Gfap
Golgi marker 130
Herg
Hif
K(v)10.1
Lpr-1
Lat-A
Mbp
Membrane
Olig2
Plp
Pm
Rsa
Snare
Soluble NSF Attachment Protein
Syn
Tca
Trapα
TfR
allograft inflammatory factor1
bungarotoxin
calcium calmodulin
calcium calmodulin kinase II
caveolin-1
detergent resistant membrane
flotilin-2
galactosylceramide
glial fibrillary acidic protein
human EAG related gene, HEK, human embryonic kidney
hypoxia inducible factor
latrunculin A
lipoprotein receptor-1
monosialotetrahexosylganglioside1
myelin basic protein
oligodendrocyte transcription factor2, Mtap1, microtubule associated protein1
plasma membrane
proteolipid protein
relative specific activity
synaptophysin
transferrin receptor
translocon associated protein alpha
trichloroacetic acid
Zusammenfassung:
KV10.1 potassium channels are implicated in a variety of cellular processes including cell proliferation and tumour progression. Their expression in over 70% of human tumours makes them an attractive diagnostic and therapeutic target. Although their physiological role in the central nervous system is not yet fully understood, advances in their precise cell localization will contribute to the understanding of their interactions and function. We have determined the plasma membrane (PM) distribution of the KV10.1 protein in an enriched mouse brain PM fraction and its association with cholesterol- and sphingolipid-rich domains. We show that the KV10.1 channel has two different populations in a 3:2 ratio, one associated to and another excluded from Detergent Resistant Membranes (DRMs). This distribution of KV10.1 in isolated PM is cholesterol- and cytoskeleton-dependent since alteration of those factors changes the relationship to 1:4. In transfected HEK-293 cells with a mutant unable to bind Ca(2+)/CaM to KV10.1 protein, Kv10.1 distribution in DRM/non-DRM is 1:4. Mean current density was doubled in the cholesterol-depleted cells, without any noticeable effects on other parameters. These results demonstrate that recruitment of the KV10.1 channel to the DRM fractions involves its functional regulation.
