Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel

W. Michael Schopperle, Mats H. Holmqvist, Yi Zhou, Jing Wang, Zheng Wang, Leslie C. Griffith, Inna Keselman, Felicity Kusinitz, Daniel Dagan, Irwin B. Levitan

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSIo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSIo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila FAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat K(v)l.3. Confocal fluorescence microscopy demonstrates that Slob and dSIo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSIo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel- binding proteins.

Original languageEnglish (US)
Pages (from-to)565-573
Number of pages9
JournalNeuron
Volume20
Issue number3
DOIs
StatePublished - Jan 1 1998
Externally publishedYes

Fingerprint

Calcium-Activated Potassium Channels
Drosophila
Proteins
Potassium Channels
Fluorescence Microscopy
Confocal Microscopy
Carrier Proteins
Yeasts
Head
Membranes

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Schopperle, W. M., Holmqvist, M. H., Zhou, Y., Wang, J., Wang, Z., Griffith, L. C., ... Levitan, I. B. (1998). Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel. Neuron, 20(3), 565-573. https://doi.org/10.1016/S0896-6273(00)80995-2

Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel. / Schopperle, W. Michael; Holmqvist, Mats H.; Zhou, Yi; Wang, Jing; Wang, Zheng; Griffith, Leslie C.; Keselman, Inna; Kusinitz, Felicity; Dagan, Daniel; Levitan, Irwin B.

In: Neuron, Vol. 20, No. 3, 01.01.1998, p. 565-573.

Research output: Contribution to journalArticle

Schopperle, WM, Holmqvist, MH, Zhou, Y, Wang, J, Wang, Z, Griffith, LC, Keselman, I, Kusinitz, F, Dagan, D & Levitan, IB 1998, 'Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel', Neuron, vol. 20, no. 3, pp. 565-573. https://doi.org/10.1016/S0896-6273(00)80995-2
Schopperle WM, Holmqvist MH, Zhou Y, Wang J, Wang Z, Griffith LC et al. Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel. Neuron. 1998 Jan 1;20(3):565-573. https://doi.org/10.1016/S0896-6273(00)80995-2
Schopperle, W. Michael ; Holmqvist, Mats H. ; Zhou, Yi ; Wang, Jing ; Wang, Zheng ; Griffith, Leslie C. ; Keselman, Inna ; Kusinitz, Felicity ; Dagan, Daniel ; Levitan, Irwin B. / Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel. In: Neuron. 1998 ; Vol. 20, No. 3. pp. 565-573.
@article{a769908253184d09ba34a3401bf45c51,
title = "Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel",
abstract = "Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSIo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSIo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila FAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat K(v)l.3. Confocal fluorescence microscopy demonstrates that Slob and dSIo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSIo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel- binding proteins.",
author = "Schopperle, {W. Michael} and Holmqvist, {Mats H.} and Yi Zhou and Jing Wang and Zheng Wang and Griffith, {Leslie C.} and Inna Keselman and Felicity Kusinitz and Daniel Dagan and Levitan, {Irwin B.}",
year = "1998",
month = "1",
day = "1",
doi = "10.1016/S0896-6273(00)80995-2",
language = "English (US)",
volume = "20",
pages = "565--573",
journal = "Neuron",
issn = "0896-6273",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - Slob, a novel protein that interacts with the slowpoke calcium-dependent potassium channel

AU - Schopperle, W. Michael

AU - Holmqvist, Mats H.

AU - Zhou, Yi

AU - Wang, Jing

AU - Wang, Zheng

AU - Griffith, Leslie C.

AU - Keselman, Inna

AU - Kusinitz, Felicity

AU - Dagan, Daniel

AU - Levitan, Irwin B.

PY - 1998/1/1

Y1 - 1998/1/1

N2 - Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSIo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSIo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila FAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat K(v)l.3. Confocal fluorescence microscopy demonstrates that Slob and dSIo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSIo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel- binding proteins.

AB - Slob, a novel protein that binds to the carboxy-terminal domain of the Drosophila Slowpoke (dSIo) calcium-dependent potassium channel, was identified with a yeast two-hybrid screen. Slob and dSIo coimmunoprecipitate from Drosophila heads and heterologous host cells, suggesting that they interact in vivo. Slob also coimmunoprecipitates with the Drosophila FAG potassium channel but not with Drosophila Shaker, mouse Slowpoke, or rat K(v)l.3. Confocal fluorescence microscopy demonstrates that Slob and dSIo redistribute in cotransfected cells and are colocalized in large intracellular structures. Direct application of Slob to the cytoplasmic face of detached membrane patches containing dSIo channels leads to an increase in channel activity. Slob may represent a new class of multi-functional channel- binding proteins.

UR - http://www.scopus.com/inward/record.url?scp=0032032849&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032032849&partnerID=8YFLogxK

U2 - 10.1016/S0896-6273(00)80995-2

DO - 10.1016/S0896-6273(00)80995-2

M3 - Article

VL - 20

SP - 565

EP - 573

JO - Neuron

JF - Neuron

SN - 0896-6273

IS - 3

ER -