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Assembly and trafficking of human small conductance Ca2+ -activated K+ channel SK3 are governed by different molecular domains.  (2005)

Authors:
Roncarati, Renza; Decimo, Ilaria; Fumagalli, Guido Francesco
Title:
Assembly and trafficking of human small conductance Ca2+ -activated K+ channel SK3 are governed by different molecular domains.
Year:
2005
Type of item:
Articolo in Rivista
Tipologia ANVUR:
Articolo su rivista
Language:
Inglese
Format:
A Stampa
Referee:
Name of journal:
MOLECULAR AND CELLULAR NEUROSCIENCES
ISSN of journal:
1044-7431
N° Volume:
28
Number or Folder:
2
Page numbers:
314-325
Keyword:
ACTIVATED POTASSIUM CHANNELS; CELL-SURFACE EXPRESSION; HIPPOCAMPAL-NEURONS; RAT-BRAIN; CURRENTS; AFTERHYPERPOLARIZATION
Short description of contents:
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.
Product ID:
24930
Handle IRIS:
11562/24930
Deposited On:
March 16, 2012
Last Modified:
October 31, 2020
Bibliographic citation:
Roncarati, Renza; Decimo, Ilaria; Fumagalli, Guido Francesco, Assembly and trafficking of human small conductance Ca2+ -activated K+ channel SK3 are governed by different molecular domains. «MOLECULAR AND CELLULAR NEUROSCIENCES» , vol. 28 , n. 22005pp. 314-325

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