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Molecular and cellular neuroscience, 2005-02, Vol.28 (2), p.314-325
2005
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Autor(en) / Beteiligte
Titel
Assembly and trafficking of human small conductance Ca2+-activated K+ channel SK3 are governed by different molecular domains
Ist Teil von
  • Molecular and cellular neuroscience, 2005-02, Vol.28 (2), p.314-325
Ort / Verlag
United States
Erscheinungsjahr
2005
Quelle
MEDLINE
Beschreibungen/Notizen
  • Intracellular trafficking is an important event in the control of type and number of ion channels expressed on the cell surface. In this study, we have identified molecular domains involved in assembly and trafficking of the human small conductance Ca2+-activated K+ channel SK3. Deletion of the N-terminus, the C-terminus, or the calmodulin-binding domain (CaMBD) led to retention of SK3 channels in the endoplasmic reticulum. Presence of the CaMBD allowed trafficking to the Golgi complex, and sequences downstream were required for efficient transport to the plasma membrane, suggesting several steps in the control of SK3 forward trafficking. Co-immunoprecipitation studies demonstrated that SK3 subunits lacking the N-terminus, the CaMBD, or the distal C-terminus, but not the entire C-terminus, were able to oligomerize with wild-type SK3 subunits. Thus, these two C-terminal regions of SK3 seem to contribute to assembly and trafficking of channels whereas the N-terminus is necessary for trafficking but not sufficient for oligomerization.

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