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

doi:10.1016/j.bbrc.2008.09.034

Modulation of Ca_v3.1 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 journal › Article › peer-review

15 Citations (Scopus)

Abstract

In order to study the currently unknown cellular signaling pathways of Ca_v3.1 T-type Ca²⁺ channels (Ca_v3.1 channels), we performed a yeast two-hybrid screening using intracellular domains of Ca_v3.1 α1 subunit as bait. After screening the human brain cDNA library, several proteins, including RanBPM, were identified as interacting with Ca_v3.1 channels. RanBPM was found to bind to the cytoplasmic intracellular loop between transmembrane domains I and II of Ca_v3.1 channels. Using whole-cell patch-clamp techniques, we found that Ca_v3.1 currents were increased by the expression of RanBPM in HEK293/Ca_v3.1 cells. We next examined whether RanBPM affected the biophysical properties and plasma membrane expression of Ca_v3.1 channels. Furthermore, we showed that the PKC activator inhibited Ca_v3.1 currents, an effect that was abolished by the expression of RanBPM. These results suggest that RanBPM could be a key regulator of Ca_v3.1 channel-mediated signaling pathways.

Original language	English
Pages (from-to)	15-20
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	378
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2008.09.034
Publication status	Published - 2009 Jan 2

Bibliographical note

Funding Information:
This work was supported by KIST Vision 21 Program, KIST Core-Competence Program, and Brain Research Center of the 21st Century Frontier Research Program (M103KV010007-08K2201-00710 to H.R.), the Republic of Korea. The authors extend their appreciation to Drs. Nishimoto and Bianchi for providing RanBPM plasmid and to Dr. Perez-Reyes for HEK293/Ca v 3.1 cells.

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2008.09.034

Cite this

@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",

note = "Funding Information: This work was supported by KIST Vision 21 Program, KIST Core-Competence Program, and Brain Research Center of the 21st Century Frontier Research Program (M103KV010007-08K2201-00710 to H.R.), the Republic of Korea. The authors extend their appreciation to Drs. Nishimoto and Bianchi for providing RanBPM plasmid and to Dr. Perez-Reyes for HEK293/Ca v 3.1 cells. ",

year = "2009",

month = jan,

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",

}

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

N1 - Funding Information: This work was supported by KIST Vision 21 Program, KIST Core-Competence Program, and Brain Research Center of the 21st Century Frontier Research Program (M103KV010007-08K2201-00710 to H.R.), the Republic of Korea. The authors extend their appreciation to Drs. Nishimoto and Bianchi for providing RanBPM plasmid and to Dr. Perez-Reyes for HEK293/Ca v 3.1 cells.

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

C2 - 18801335

AN - SCOPUS:57049140013

SN - 0006-291X

VL - 378

SP - 15

EP - 20

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -