Phalloidin and tropomyosin do not prevent actin filament shortening by the 90 kD protein-actin complex from brain

A. B. Verkhovsky; I. G. Surgucheva; V. I. Gelfand

doi:10.1016/0006-291X(84)90271-7

Phalloidin and tropomyosin do not prevent actin filament shortening by the 90 kD protein-actin complex from brain

A. B. Verkhovsky^*, I. G. Surgucheva, V. I. Gelfand

^*Corresponding author for this work

Cell & Developmental Biology

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

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Abstract

Previously we reported the purification from bovine brain of the 90 kD protein-actin complex that shortens actin filaments. In the present work we study the effect of this complex on actin polymerized in the presence of phalloidin (PL) or tropomyosin (TM) which are known to stabilize actin filaments. The effect of the complex has been compared with that of cytochalasin D (CD), a fungal metabolite that also shortens actin filaments. Low shear viscosimetry and electron microscopy showed that PL or TM could not prevent the shortening of actin filaments in the presence of 90 kD protein-actin complex whereas they effectively protected actin filaments from shortening by CD. We conclude that the 90 kD protein-actin complex is a more potent filament-shortening factor than CD.

Original language	English (US)
Pages (from-to)	596-603
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	123
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(84)90271-7
State	Published - Sep 17 1984

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Phalloidin and tropomyosin do not prevent actin filament shortening by the 90 kD protein-actin complex from brain",

abstract = "Previously we reported the purification from bovine brain of the 90 kD protein-actin complex that shortens actin filaments. In the present work we study the effect of this complex on actin polymerized in the presence of phalloidin (PL) or tropomyosin (TM) which are known to stabilize actin filaments. The effect of the complex has been compared with that of cytochalasin D (CD), a fungal metabolite that also shortens actin filaments. Low shear viscosimetry and electron microscopy showed that PL or TM could not prevent the shortening of actin filaments in the presence of 90 kD protein-actin complex whereas they effectively protected actin filaments from shortening by CD. We conclude that the 90 kD protein-actin complex is a more potent filament-shortening factor than CD.",

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AU - Verkhovsky, A. B.

AU - Surgucheva, I. G.

AU - Gelfand, V. I.

PY - 1984/9/17

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AB - Previously we reported the purification from bovine brain of the 90 kD protein-actin complex that shortens actin filaments. In the present work we study the effect of this complex on actin polymerized in the presence of phalloidin (PL) or tropomyosin (TM) which are known to stabilize actin filaments. The effect of the complex has been compared with that of cytochalasin D (CD), a fungal metabolite that also shortens actin filaments. Low shear viscosimetry and electron microscopy showed that PL or TM could not prevent the shortening of actin filaments in the presence of 90 kD protein-actin complex whereas they effectively protected actin filaments from shortening by CD. We conclude that the 90 kD protein-actin complex is a more potent filament-shortening factor than CD.

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Phalloidin and tropomyosin do not prevent actin filament shortening by the 90 kD protein-actin complex from brain

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