Regulation of CapZ, an Actin Capping Protein of Chicken Muscle, by Anionic Phospholipids

Steven G. Heiss; John A. Cooper

doi:10.1021/bi00100a006

Regulation of CapZ, an Actin Capping Protein of Chicken Muscle, by Anionic Phospholipids

Steven G. Heiss, John A. Cooper

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

96 Scopus citations

Abstract

Chicken muscle CapZ, a member of the capping protein family of actin-binding proteins, binds to the barbed end of actin filaments and nucleates actin polymerization. No regulation of the capping protein family has been described. We report that micelles of phosphatidylinositol 4,5-bisphosphate (PIP2) bind to CapZ and completely inhibit its ability to affect actin polymerization as measured by several independent assays. Higher concentrations of other anionic phospholipids also completely inhibit the activity of CapZ. Neutral phospholipids have no effect. Mixed vesicles of PIP₂ with phosphatidylcholine or phosphatidyl-ethanolamine also inhibit CapZ, but addition of Triton X-100 both prevents and reverses PIP₂'s inhibition of CapZ.

Original language	English
Pages (from-to)	8753-8758
Number of pages	6
Journal	Biochemistry
Volume	30
Issue number	36
DOIs	https://doi.org/10.1021/bi00100a006
State	Published - Sep 1 1991

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abstract = "Chicken muscle CapZ, a member of the capping protein family of actin-binding proteins, binds to the barbed end of actin filaments and nucleates actin polymerization. No regulation of the capping protein family has been described. We report that micelles of phosphatidylinositol 4,5-bisphosphate (PIP2) bind to CapZ and completely inhibit its ability to affect actin polymerization as measured by several independent assays. Higher concentrations of other anionic phospholipids also completely inhibit the activity of CapZ. Neutral phospholipids have no effect. Mixed vesicles of PIP2 with phosphatidylcholine or phosphatidyl-ethanolamine also inhibit CapZ, but addition of Triton X-100 both prevents and reverses PIP2's inhibition of CapZ.",

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T1 - Regulation of CapZ, an Actin Capping Protein of Chicken Muscle, by Anionic Phospholipids

AU - Heiss, Steven G.

AU - Cooper, John A.

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N2 - Chicken muscle CapZ, a member of the capping protein family of actin-binding proteins, binds to the barbed end of actin filaments and nucleates actin polymerization. No regulation of the capping protein family has been described. We report that micelles of phosphatidylinositol 4,5-bisphosphate (PIP2) bind to CapZ and completely inhibit its ability to affect actin polymerization as measured by several independent assays. Higher concentrations of other anionic phospholipids also completely inhibit the activity of CapZ. Neutral phospholipids have no effect. Mixed vesicles of PIP2 with phosphatidylcholine or phosphatidyl-ethanolamine also inhibit CapZ, but addition of Triton X-100 both prevents and reverses PIP2's inhibition of CapZ.

AB - Chicken muscle CapZ, a member of the capping protein family of actin-binding proteins, binds to the barbed end of actin filaments and nucleates actin polymerization. No regulation of the capping protein family has been described. We report that micelles of phosphatidylinositol 4,5-bisphosphate (PIP2) bind to CapZ and completely inhibit its ability to affect actin polymerization as measured by several independent assays. Higher concentrations of other anionic phospholipids also completely inhibit the activity of CapZ. Neutral phospholipids have no effect. Mixed vesicles of PIP2 with phosphatidylcholine or phosphatidyl-ethanolamine also inhibit CapZ, but addition of Triton X-100 both prevents and reverses PIP2's inhibition of CapZ.

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JO - Biochemistry

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ER -

Regulation of CapZ, an Actin Capping Protein of Chicken Muscle, by Anionic Phospholipids

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