Modulation of Cav3.1 T-type Ca2+ channels by the ran binding protein RanBPM

Taehyun Kim, Sunoh Kim, Hyung Mun Yun, Kwang Chul Chung, Ye Sun Han, Hee Sup Shin, Hyewhon Rhim

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

In order to study the currently unknown cellular signaling pathways of Cav3.1 T-type Ca2+ channels (Cav3.1 channels), we performed a yeast two-hybrid screening using intracellular domains of Cav3.1 α1 subunit as bait. After screening the human brain cDNA library, several proteins, including RanBPM, were identified as interacting with Cav3.1 channels. RanBPM was found to bind to the cytoplasmic intracellular loop between transmembrane domains I and II of Cav3.1 channels. Using whole-cell patch-clamp techniques, we found that Cav3.1 currents were increased by the expression of RanBPM in HEK293/Cav3.1 cells. We next examined whether RanBPM affected the biophysical properties and plasma membrane expression of Cav3.1 channels. Furthermore, we showed that the PKC activator inhibited Cav3.1 currents, an effect that was abolished by the expression of RanBPM. These results suggest that RanBPM could be a key regulator of Cav3.1 channel-mediated signaling pathways.

Original languageEnglish
Pages (from-to)15-20
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume378
Issue number1
DOIs
Publication statusPublished - 2009 Jan 2

Fingerprint

ran GTP-Binding Protein
Carrier Proteins
Modulation
Screening
Cell signaling
HEK293 Cells
Clamping devices
Patch-Clamp Techniques
Cell membranes
Gene Library
Yeast
Ran binding protein 9
Brain
Yeasts
Cell Membrane

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Kim, Taehyun ; Kim, Sunoh ; Yun, Hyung Mun ; Chung, Kwang Chul ; Han, Ye Sun ; Shin, Hee Sup ; Rhim, Hyewhon. / Modulation of Cav3.1 T-type Ca2+ channels by the ran binding protein RanBPM. In: Biochemical and Biophysical Research Communications. 2009 ; Vol. 378, No. 1. pp. 15-20.
@article{3aa81ed4d6b241ee87ceea2cd4666fbe,
title = "Modulation of Cav3.1 T-type Ca2+ channels by the ran binding protein RanBPM",
abstract = "In order to study the currently unknown cellular signaling pathways of Cav3.1 T-type Ca2+ channels (Cav3.1 channels), we performed a yeast two-hybrid screening using intracellular domains of Cav3.1 α1 subunit as bait. After screening the human brain cDNA library, several proteins, including RanBPM, were identified as interacting with Cav3.1 channels. RanBPM was found to bind to the cytoplasmic intracellular loop between transmembrane domains I and II of Cav3.1 channels. Using whole-cell patch-clamp techniques, we found that Cav3.1 currents were increased by the expression of RanBPM in HEK293/Cav3.1 cells. We next examined whether RanBPM affected the biophysical properties and plasma membrane expression of Cav3.1 channels. Furthermore, we showed that the PKC activator inhibited Cav3.1 currents, an effect that was abolished by the expression of RanBPM. These results suggest that RanBPM could be a key regulator of Cav3.1 channel-mediated signaling pathways.",
author = "Taehyun Kim and Sunoh Kim and Yun, {Hyung Mun} and Chung, {Kwang Chul} and Han, {Ye Sun} and Shin, {Hee Sup} and Hyewhon Rhim",
year = "2009",
month = "1",
day = "2",
doi = "10.1016/j.bbrc.2008.09.034",
language = "English",
volume = "378",
pages = "15--20",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

Modulation of Cav3.1 T-type Ca2+ channels by the ran binding protein RanBPM. / Kim, Taehyun; Kim, Sunoh; Yun, Hyung Mun; Chung, Kwang Chul; Han, Ye Sun; Shin, Hee Sup; Rhim, Hyewhon.

In: Biochemical and Biophysical Research Communications, Vol. 378, No. 1, 02.01.2009, p. 15-20.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Modulation of Cav3.1 T-type Ca2+ channels by the ran binding protein RanBPM

AU - Kim, Taehyun

AU - Kim, Sunoh

AU - Yun, Hyung Mun

AU - Chung, Kwang Chul

AU - Han, Ye Sun

AU - Shin, Hee Sup

AU - Rhim, Hyewhon

PY - 2009/1/2

Y1 - 2009/1/2

N2 - In order to study the currently unknown cellular signaling pathways of Cav3.1 T-type Ca2+ channels (Cav3.1 channels), we performed a yeast two-hybrid screening using intracellular domains of Cav3.1 α1 subunit as bait. After screening the human brain cDNA library, several proteins, including RanBPM, were identified as interacting with Cav3.1 channels. RanBPM was found to bind to the cytoplasmic intracellular loop between transmembrane domains I and II of Cav3.1 channels. Using whole-cell patch-clamp techniques, we found that Cav3.1 currents were increased by the expression of RanBPM in HEK293/Cav3.1 cells. We next examined whether RanBPM affected the biophysical properties and plasma membrane expression of Cav3.1 channels. Furthermore, we showed that the PKC activator inhibited Cav3.1 currents, an effect that was abolished by the expression of RanBPM. These results suggest that RanBPM could be a key regulator of Cav3.1 channel-mediated signaling pathways.

AB - In order to study the currently unknown cellular signaling pathways of Cav3.1 T-type Ca2+ channels (Cav3.1 channels), we performed a yeast two-hybrid screening using intracellular domains of Cav3.1 α1 subunit as bait. After screening the human brain cDNA library, several proteins, including RanBPM, were identified as interacting with Cav3.1 channels. RanBPM was found to bind to the cytoplasmic intracellular loop between transmembrane domains I and II of Cav3.1 channels. Using whole-cell patch-clamp techniques, we found that Cav3.1 currents were increased by the expression of RanBPM in HEK293/Cav3.1 cells. We next examined whether RanBPM affected the biophysical properties and plasma membrane expression of Cav3.1 channels. Furthermore, we showed that the PKC activator inhibited Cav3.1 currents, an effect that was abolished by the expression of RanBPM. These results suggest that RanBPM could be a key regulator of Cav3.1 channel-mediated signaling pathways.

UR - http://www.scopus.com/inward/record.url?scp=57049140013&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=57049140013&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2008.09.034

DO - 10.1016/j.bbrc.2008.09.034

M3 - Article

VL - 378

SP - 15

EP - 20

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -