The modular structure of actin-regulatory proteins

Yoram A. Puius, Nicole M. Mahoney, Steven C. Almo

Research output: Contribution to journalArticle

106 Citations (Scopus)

Abstract

Filamentous actin structures possess unique biophysical and biochemical properties and are required for cell locomotion, cell division, compartmentalization and morphological processes. The site-specific assembly and disassembly of these structures are directed by actin-regulatory proteins. This article reviews how structural studies are now defining the atomic details of small modular domains present in actin-regulatory proteins responsible for crosslinking, severing and capping of actin filaments, as well as for localization of actin filament assembly. These studies have identified three modular strategies for the design of proteins that regulate the actin cytoskeleton.

Original languageEnglish (US)
Pages (from-to)23-34
Number of pages12
JournalCurrent Opinion in Cell Biology
Volume10
Issue number1
DOIs
StatePublished - Feb 1998

Fingerprint

Actin Cytoskeleton
Actins
Proteins
Cell Division
Cell Movement

ASJC Scopus subject areas

  • Cell Biology

Cite this

The modular structure of actin-regulatory proteins. / Puius, Yoram A.; Mahoney, Nicole M.; Almo, Steven C.

In: Current Opinion in Cell Biology, Vol. 10, No. 1, 02.1998, p. 23-34.

Research output: Contribution to journalArticle

@article{972b25fc38ac4e1b978f3c522c71cfba,
title = "The modular structure of actin-regulatory proteins",
abstract = "Filamentous actin structures possess unique biophysical and biochemical properties and are required for cell locomotion, cell division, compartmentalization and morphological processes. The site-specific assembly and disassembly of these structures are directed by actin-regulatory proteins. This article reviews how structural studies are now defining the atomic details of small modular domains present in actin-regulatory proteins responsible for crosslinking, severing and capping of actin filaments, as well as for localization of actin filament assembly. These studies have identified three modular strategies for the design of proteins that regulate the actin cytoskeleton.",
author = "Puius, {Yoram A.} and Mahoney, {Nicole M.} and Almo, {Steven C.}",
year = "1998",
month = "2",
doi = "10.1016/S0955-0674(98)80083-5",
language = "English (US)",
volume = "10",
pages = "23--34",
journal = "Current Opinion in Cell Biology",
issn = "0955-0674",
publisher = "Elsevier Limited",
number = "1",

}

TY - JOUR

T1 - The modular structure of actin-regulatory proteins

AU - Puius, Yoram A.

AU - Mahoney, Nicole M.

AU - Almo, Steven C.

PY - 1998/2

Y1 - 1998/2

N2 - Filamentous actin structures possess unique biophysical and biochemical properties and are required for cell locomotion, cell division, compartmentalization and morphological processes. The site-specific assembly and disassembly of these structures are directed by actin-regulatory proteins. This article reviews how structural studies are now defining the atomic details of small modular domains present in actin-regulatory proteins responsible for crosslinking, severing and capping of actin filaments, as well as for localization of actin filament assembly. These studies have identified three modular strategies for the design of proteins that regulate the actin cytoskeleton.

AB - Filamentous actin structures possess unique biophysical and biochemical properties and are required for cell locomotion, cell division, compartmentalization and morphological processes. The site-specific assembly and disassembly of these structures are directed by actin-regulatory proteins. This article reviews how structural studies are now defining the atomic details of small modular domains present in actin-regulatory proteins responsible for crosslinking, severing and capping of actin filaments, as well as for localization of actin filament assembly. These studies have identified three modular strategies for the design of proteins that regulate the actin cytoskeleton.

UR - http://www.scopus.com/inward/record.url?scp=0032005974&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032005974&partnerID=8YFLogxK

U2 - 10.1016/S0955-0674(98)80083-5

DO - 10.1016/S0955-0674(98)80083-5

M3 - Article

C2 - 9484592

AN - SCOPUS:0032005974

VL - 10

SP - 23

EP - 34

JO - Current Opinion in Cell Biology

JF - Current Opinion in Cell Biology

SN - 0955-0674

IS - 1

ER -