Abstract
The voltage-sensitive K+ channel Kv2.1 has a polarized and clustered distribution in neurons. To investigate the basis for this localization, we expressed wild-type Kv2.1 and two COOH-terminal truncation mutants, ΔC318 and ΔC187, in polarized epithelial MDCK cells. These functional channel proteins had differing subcellular localization, in that while both wild- type Kv2.1 and ΔC187 localized to the lateral membrane in high density clusters, ΔC318 was expressed uniformly on both apical and lateral membranes. A chimeric protein containing the hemagglutin in protein from influenza virus and the region of Kv2.1 that differentiates the two truncation mutants (amino acids 536-666) was also expressed in MDCK cells, where it was found in high density clusters similar to those observed for Kv2.1. Polarized expression and clustering of Kv2.1 correlates with detergent solubility, suggesting that interaction with the detergent insoluble cytoskeleton may be necessary for proper localization of this channel.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1619-1632 |
| Number of pages | 14 |
| Journal | Journal of Cell Biology |
| Volume | 135 |
| Issue number | 6 |
| DOIs | |
| State | Published - 1996 |
| Externally published | Yes |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
Cite this
Identification of a cytoplasmic domain important in the polarized expression and clustering of the Kv2.1 K+ channel. / Scannevin, Robert H.; Murakoshi, Hideyuki; Rhodes, Kenneth J.; Trimmer, James.
In: Journal of Cell Biology, Vol. 135, No. 6, 1996, p. 1619-1632.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of a cytoplasmic domain important in the polarized expression and clustering of the Kv2.1 K+ channel
AU - Scannevin, Robert H.
AU - Murakoshi, Hideyuki
AU - Rhodes, Kenneth J.
AU - Trimmer, James
PY - 1996
Y1 - 1996
N2 - The voltage-sensitive K+ channel Kv2.1 has a polarized and clustered distribution in neurons. To investigate the basis for this localization, we expressed wild-type Kv2.1 and two COOH-terminal truncation mutants, ΔC318 and ΔC187, in polarized epithelial MDCK cells. These functional channel proteins had differing subcellular localization, in that while both wild- type Kv2.1 and ΔC187 localized to the lateral membrane in high density clusters, ΔC318 was expressed uniformly on both apical and lateral membranes. A chimeric protein containing the hemagglutin in protein from influenza virus and the region of Kv2.1 that differentiates the two truncation mutants (amino acids 536-666) was also expressed in MDCK cells, where it was found in high density clusters similar to those observed for Kv2.1. Polarized expression and clustering of Kv2.1 correlates with detergent solubility, suggesting that interaction with the detergent insoluble cytoskeleton may be necessary for proper localization of this channel.
AB - The voltage-sensitive K+ channel Kv2.1 has a polarized and clustered distribution in neurons. To investigate the basis for this localization, we expressed wild-type Kv2.1 and two COOH-terminal truncation mutants, ΔC318 and ΔC187, in polarized epithelial MDCK cells. These functional channel proteins had differing subcellular localization, in that while both wild- type Kv2.1 and ΔC187 localized to the lateral membrane in high density clusters, ΔC318 was expressed uniformly on both apical and lateral membranes. A chimeric protein containing the hemagglutin in protein from influenza virus and the region of Kv2.1 that differentiates the two truncation mutants (amino acids 536-666) was also expressed in MDCK cells, where it was found in high density clusters similar to those observed for Kv2.1. Polarized expression and clustering of Kv2.1 correlates with detergent solubility, suggesting that interaction with the detergent insoluble cytoskeleton may be necessary for proper localization of this channel.
UR - http://www.scopus.com/inward/record.url?scp=0030453193&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030453193&partnerID=8YFLogxK
U2 - 10.1083/jcb.135.6.1619
DO - 10.1083/jcb.135.6.1619
M3 - Article
C2 - 8978827
AN - SCOPUS:0030453193
VL - 135
SP - 1619
EP - 1632
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 6
ER -