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The retention factor p11 confers an endoplasmic reticulum-localization signal to the potassium channel TASK-1.
- Source :
-
Traffic (Copenhagen, Denmark) [Traffic] 2006 Feb; Vol. 7 (2), pp. 168-81. - Publication Year :
- 2006
-
Abstract
- The interaction of the adaptor protein p11, also denoted S100A10, with the C-terminus of the two-pore-domain K+ channel TASK-1 was studied using yeast two-hybrid analysis, glutathione S-transferase pull-down, and co-immunoprecipitation. We found that p11 interacts with a 40 amino-acid region in the proximal C-terminus of the channel. In heterologous expression systems, deletion of the p11-interacting domain enhanced surface expression of TASK-1. Attachment of the p11-interacting domain to the cytosolic tail of the reporter protein CD8 caused retention/retrieval of the construct in the endoplasmic reticulum (ER). Attachment of the last 36 amino acids of p11 to CD8 also caused ER localization, which was abolished by removal or mutation of a putative retention motif (H/K)xKxxx, at the C-terminal end of p11. Imaging of EGFP-tagged TASK-1 channels in COS cells suggested that wild-type TASK-1 was largely retained in the ER. Knockdown of p11 with siRNA enhanced trafficking of TASK-1 to the surface membrane. Our results suggest that binding of p11 to TASK-1 retards the surface expression of the channel, most likely by virtue of a di-lysine retention signal at the C-terminus of p11. Thus, the cytosolic protein p11 may represent a 'retention factor' that causes localization of the channel to the ER.
- Subjects :
- 14-3-3 Proteins chemistry
14-3-3 Proteins genetics
14-3-3 Proteins metabolism
Amino Acid Sequence
Animals
Annexin A2 chemistry
Annexin A2 genetics
Binding Sites genetics
CD8 Antigens chemistry
CD8 Antigens genetics
CD8 Antigens metabolism
CHO Cells
COS Cells
Cell Line
Chlorocebus aethiops
Cricetinae
Female
Humans
In Vitro Techniques
Models, Biological
Molecular Sequence Data
Mutagenesis, Site-Directed
Nerve Tissue Proteins
Oocytes metabolism
Potassium Channels, Tandem Pore Domain chemistry
Potassium Channels, Tandem Pore Domain genetics
Protein Structure, Tertiary
RNA Interference
RNA, Small Interfering genetics
Rats
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
S100 Proteins chemistry
S100 Proteins genetics
Sequence Homology, Amino Acid
Two-Hybrid System Techniques
Xenopus
Annexin A2 metabolism
Endoplasmic Reticulum metabolism
Potassium Channels, Tandem Pore Domain metabolism
S100 Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1398-9219
- Volume :
- 7
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Traffic (Copenhagen, Denmark)
- Publication Type :
- Academic Journal
- Accession number :
- 16420525
- Full Text :
- https://doi.org/10.1111/j.1600-0854.2005.00375.x