The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins

Adeleke H. Aguda, Bo Xue, Edward Irobi, Thomas Préat, Robert C. Robinson

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/β-thymosin (βT) domain. WH2/βT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/βT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the βT and WH2 motifs are not functionally analogous.

Original languageEnglish
Pages (from-to)469-476
Number of pages8
JournalStructure
Volume14
Issue number3
DOIs
Publication statusPublished - Mar 1 2006
Externally publishedYes

Fingerprint

Thymosin
Amino Acid Motifs
Actins
Wiskott-Aldrich Syndrome
Proteins
Wiskott-Aldrich Syndrome Protein
Profilins
Gelsolin
Actin Cytoskeleton
Drosophila ciboulot protein

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins. / Aguda, Adeleke H.; Xue, Bo; Irobi, Edward; Préat, Thomas; Robinson, Robert C.

In: Structure, Vol. 14, No. 3, 01.03.2006, p. 469-476.

Research output: Contribution to journalArticle

Aguda, Adeleke H. ; Xue, Bo ; Irobi, Edward ; Préat, Thomas ; Robinson, Robert C. / The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins. In: Structure. 2006 ; Vol. 14, No. 3. pp. 469-476.
@article{3efbcf8106914ee2a333f1dbc0b1ddd6,
title = "The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins",
abstract = "Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/β-thymosin (βT) domain. WH2/βT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/βT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the βT and WH2 motifs are not functionally analogous.",
author = "Aguda, {Adeleke H.} and Bo Xue and Edward Irobi and Thomas Pr{\'e}at and Robinson, {Robert C.}",
year = "2006",
month = "3",
day = "1",
doi = "10.1016/j.str.2005.12.011",
language = "English",
volume = "14",
pages = "469--476",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - The structural basis of actin interaction with multiple WH2/β-thymosin motif-containing proteins

AU - Aguda, Adeleke H.

AU - Xue, Bo

AU - Irobi, Edward

AU - Préat, Thomas

AU - Robinson, Robert C.

PY - 2006/3/1

Y1 - 2006/3/1

N2 - Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/β-thymosin (βT) domain. WH2/βT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/βT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the βT and WH2 motifs are not functionally analogous.

AB - Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/β-thymosin (βT) domain. WH2/βT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/βT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the βT and WH2 motifs are not functionally analogous.

UR - http://www.scopus.com/inward/record.url?scp=33644835262&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33644835262&partnerID=8YFLogxK

U2 - 10.1016/j.str.2005.12.011

DO - 10.1016/j.str.2005.12.011

M3 - Article

C2 - 16531231

AN - SCOPUS:33644835262

VL - 14

SP - 469

EP - 476

JO - Structure with Folding & design

JF - Structure with Folding & design

SN - 0969-2126

IS - 3

ER -