Protein kinase Cα can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway

Hyowon Son; Yangmi Lim; Jinsook Kim; Haein Park; Sojoong Choi; Innoc Han; Won Seok Kim; Sungsu Park; Yunsoo Bae; Eok Soo Oh

doi:10.1016/j.abb.2006.08.013

Protein kinase Cα can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway

Hyowon Son, Yangmi Lim, Jinsook Kim, Haein Park, Sojoong Choi, Innoc Han, Won Seok Kim, Sungsu Park, Yunsoo Bae, Eok Soo Oh

Department of Life Science

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Protein kinase Cα (PKCα) activation is known to be dependent on the metabolic product of phosphatidylinositol 4,5-bisphosphate (PIP₂) by phospholipase C (PLC). Here we report that fibroblasts may have an additional PIP₂-dependent mechanism for membrane localization of PKCα. We observed PKCα membrane localization in both wild type and PLCγ1 -/- mouse embryonic fibroblasts. Treatment of cells with a specific PLC inhibitor U73122 resulted in increased PIP₂ levels and enhanced membrane localization of PKCα. PKCα levels in the membrane fraction decreased following incubation with PLCγ, but increased following treatment with U73122 or addition of exogenous PIP₂ in vitro. In addition, PKCα interacted with PIP₂-conjugate bead and mixed micelles containing PIP₂. Finally, we found that PIP₂ is involved in syndecan-4-mediated membrane localization of PKCα. Taken together, these data suggest that PIP₂ might contribute to directly regulating the membrane localization of PKCα.

Original language	English
Pages (from-to)	1-6
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	454
Issue number	1
DOIs	https://doi.org/10.1016/j.abb.2006.08.013
State	Published - 1 Oct 2006

Bibliographical note

Funding Information:
This work was supported by Korea Research Foundation Grant (KRF-2002-CP0327 to E.S.O) and in part by Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University.

Keywords

Cytoskeleton
Membrane localization
Phosphatidylinositol 4,5-bisphosphate
Protein kinase C
Syndecan-4

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title = "Protein kinase Cα can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway",

abstract = "Protein kinase Cα (PKCα) activation is known to be dependent on the metabolic product of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C (PLC). Here we report that fibroblasts may have an additional PIP2-dependent mechanism for membrane localization of PKCα. We observed PKCα membrane localization in both wild type and PLCγ1 -/- mouse embryonic fibroblasts. Treatment of cells with a specific PLC inhibitor U73122 resulted in increased PIP2 levels and enhanced membrane localization of PKCα. PKCα levels in the membrane fraction decreased following incubation with PLCγ, but increased following treatment with U73122 or addition of exogenous PIP2 in vitro. In addition, PKCα interacted with PIP2-conjugate bead and mixed micelles containing PIP2. Finally, we found that PIP2 is involved in syndecan-4-mediated membrane localization of PKCα. Taken together, these data suggest that PIP2 might contribute to directly regulating the membrane localization of PKCα.",

keywords = "Cytoskeleton, Membrane localization, Phosphatidylinositol 4,5-bisphosphate, Protein kinase C, Syndecan-4",

author = "Hyowon Son and Yangmi Lim and Jinsook Kim and Haein Park and Sojoong Choi and Innoc Han and Kim, {Won Seok} and Sungsu Park and Yunsoo Bae and Oh, {Eok Soo}",

note = "Funding Information: This work was supported by Korea Research Foundation Grant (KRF-2002-CP0327 to E.S.O) and in part by Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University.",

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T1 - Protein kinase Cα can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway

AU - Son, Hyowon

AU - Lim, Yangmi

AU - Kim, Jinsook

AU - Park, Haein

AU - Choi, Sojoong

AU - Han, Innoc

AU - Kim, Won Seok

AU - Park, Sungsu

AU - Bae, Yunsoo

AU - Oh, Eok Soo

N1 - Funding Information: This work was supported by Korea Research Foundation Grant (KRF-2002-CP0327 to E.S.O) and in part by Korea Science and Engineering Foundation (KOSEF) through the Center for Cell Signaling Research at Ewha Womans University.

PY - 2006/10/1

Y1 - 2006/10/1

N2 - Protein kinase Cα (PKCα) activation is known to be dependent on the metabolic product of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C (PLC). Here we report that fibroblasts may have an additional PIP2-dependent mechanism for membrane localization of PKCα. We observed PKCα membrane localization in both wild type and PLCγ1 -/- mouse embryonic fibroblasts. Treatment of cells with a specific PLC inhibitor U73122 resulted in increased PIP2 levels and enhanced membrane localization of PKCα. PKCα levels in the membrane fraction decreased following incubation with PLCγ, but increased following treatment with U73122 or addition of exogenous PIP2 in vitro. In addition, PKCα interacted with PIP2-conjugate bead and mixed micelles containing PIP2. Finally, we found that PIP2 is involved in syndecan-4-mediated membrane localization of PKCα. Taken together, these data suggest that PIP2 might contribute to directly regulating the membrane localization of PKCα.

AB - Protein kinase Cα (PKCα) activation is known to be dependent on the metabolic product of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C (PLC). Here we report that fibroblasts may have an additional PIP2-dependent mechanism for membrane localization of PKCα. We observed PKCα membrane localization in both wild type and PLCγ1 -/- mouse embryonic fibroblasts. Treatment of cells with a specific PLC inhibitor U73122 resulted in increased PIP2 levels and enhanced membrane localization of PKCα. PKCα levels in the membrane fraction decreased following incubation with PLCγ, but increased following treatment with U73122 or addition of exogenous PIP2 in vitro. In addition, PKCα interacted with PIP2-conjugate bead and mixed micelles containing PIP2. Finally, we found that PIP2 is involved in syndecan-4-mediated membrane localization of PKCα. Taken together, these data suggest that PIP2 might contribute to directly regulating the membrane localization of PKCα.

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Protein kinase Cα can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway

Abstract

Bibliographical note

Keywords

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