Capping protein binding to actin in yeast: Biochemical mechanism and physiological relevance

Kyoungtae Kim, Atsuko Yamashita, Martin A. Wear, Yuichiro Maéda, John A. Cooper

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP α and β subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The α COOH-terminal region was more important than that of β. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.

Original languageEnglish
Pages (from-to)567-580
Number of pages14
JournalJournal of Cell Biology
Volume164
Issue number4
DOIs
Publication statusPublished - Feb 16 2004
Externally publishedYes

Fingerprint

Microfilament Proteins
Yeasts
Actins
Actin Capping Proteins
Fungal Proteins
Proteins
Actin Cytoskeleton
Protein Subunits
Mutant Proteins
Vertebrates
Phenotype

Keywords

  • Assembly
  • Cell motility
  • Cytoskeleton
  • Polymerization
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Cell Biology

Cite this

Capping protein binding to actin in yeast : Biochemical mechanism and physiological relevance. / Kim, Kyoungtae; Yamashita, Atsuko; Wear, Martin A.; Maéda, Yuichiro; Cooper, John A.

In: Journal of Cell Biology, Vol. 164, No. 4, 16.02.2004, p. 567-580.

Research output: Contribution to journalArticle

Kim, Kyoungtae ; Yamashita, Atsuko ; Wear, Martin A. ; Maéda, Yuichiro ; Cooper, John A. / Capping protein binding to actin in yeast : Biochemical mechanism and physiological relevance. In: Journal of Cell Biology. 2004 ; Vol. 164, No. 4. pp. 567-580.
@article{66a696c7941248c18769ede1b39c7d91,
title = "Capping protein binding to actin in yeast: Biochemical mechanism and physiological relevance",
abstract = "The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP α and β subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The α COOH-terminal region was more important than that of β. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.",
keywords = "Assembly, Cell motility, Cytoskeleton, Polymerization, Saccharomyces cerevisiae",
author = "Kyoungtae Kim and Atsuko Yamashita and Wear, {Martin A.} and Yuichiro Ma{\'e}da and Cooper, {John A.}",
year = "2004",
month = "2",
day = "16",
doi = "10.1083/jcb.200308061",
language = "English",
volume = "164",
pages = "567--580",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

TY - JOUR

T1 - Capping protein binding to actin in yeast

T2 - Biochemical mechanism and physiological relevance

AU - Kim, Kyoungtae

AU - Yamashita, Atsuko

AU - Wear, Martin A.

AU - Maéda, Yuichiro

AU - Cooper, John A.

PY - 2004/2/16

Y1 - 2004/2/16

N2 - The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP α and β subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The α COOH-terminal region was more important than that of β. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.

AB - The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP α and β subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The α COOH-terminal region was more important than that of β. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.

KW - Assembly

KW - Cell motility

KW - Cytoskeleton

KW - Polymerization

KW - Saccharomyces cerevisiae

UR - http://www.scopus.com/inward/record.url?scp=1242329989&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1242329989&partnerID=8YFLogxK

U2 - 10.1083/jcb.200308061

DO - 10.1083/jcb.200308061

M3 - Article

C2 - 14769858

AN - SCOPUS:1242329989

VL - 164

SP - 567

EP - 580

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 4

ER -