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  1. Article: WH2 domain: a small, versatile adapter for actin monomers.

    Paunola, Eija / Mattila, Pieta K / Lappalainen, Pekka

    FEBS letters

    2002  Volume 513, Issue 1, Page(s) 92–97

    Abstract: The actin cytoskeleton plays a central role in many cell biological processes. The structure and dynamics of the actin cytoskeleton are regulated by numerous actin-binding proteins that usually contain one of the few known actin-binding motifs. WH2 ... ...

    Abstract The actin cytoskeleton plays a central role in many cell biological processes. The structure and dynamics of the actin cytoskeleton are regulated by numerous actin-binding proteins that usually contain one of the few known actin-binding motifs. WH2 domain (WASP homology domain-2) is a approximately 35 residue actin monomer-binding motif, that is found in many different regulators of the actin cytoskeleton, including the beta-thymosins, ciboulot, WASP (Wiskott Aldrich syndrome protein), verprolin/WIP (WASP-interacting protein), Srv2/CAP (adenylyl cyclase-associated protein) and several uncharacterized proteins. The most highly conserved residues in the WH2 domain are important in beta-thymosin's interactions with actin monomers, suggesting that all WH2 domains may interact with actin monomers through similar interfaces. Our sequence database searches did not reveal any WH2 domain-containing proteins in plants. However, we found three classes of these proteins: WASP, Srv2/CAP and verprolin/WIP in yeast and animals. This suggests that the WH2 domain is an ancient actin monomer-binding motif that existed before the divergence of fungal and animal lineages.
    MeSH term(s) Actins/chemistry ; Actins/metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cytoskeletal Proteins/chemistry ; Cytoskeletal Proteins/metabolism ; Drosophila ; Drosophila Proteins ; Humans ; Microfilament Proteins/chemistry ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Nerve Tissue Proteins ; Phylogeny ; Protein Structure, Secondary ; Proteins/chemistry ; Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Thymosin/chemistry ; Thymosin/metabolism ; Wiskott-Aldrich Syndrome ; Wiskott-Aldrich Syndrome Protein
    Chemical Substances Actins ; Cytoskeletal Proteins ; Drosophila Proteins ; Microfilament Proteins ; Nerve Tissue Proteins ; Proteins ; WAS protein, human ; Wiskott-Aldrich Syndrome Protein ; cib protein, Drosophila ; Thymosin (61512-21-8)
    Language English
    Publishing date 2002-02-20
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/s0014-5793(01)03242-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.B 282: Show issues Location:
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  2. Article: Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells.

    Hotulainen, Pirta / Paunola, Eija / Vartiainen, Maria K / Lappalainen, Pekka

    Molecular biology of the cell

    2005  Volume 16, Issue 2, Page(s) 649–664

    Abstract: Actin-depolymerizing factor (ADF)/cofilins are small actin-binding proteins found in all eukaryotes. In vitro, ADF/cofilins promote actin dynamics by depolymerizing and severing actin filaments. However, whether ADF/cofilins contribute to actin dynamics ... ...

    Abstract Actin-depolymerizing factor (ADF)/cofilins are small actin-binding proteins found in all eukaryotes. In vitro, ADF/cofilins promote actin dynamics by depolymerizing and severing actin filaments. However, whether ADF/cofilins contribute to actin dynamics in cells by disassembling "old" actin filaments or by promoting actin filament assembly through their severing activity is a matter of controversy. Analysis of mammalian ADF/cofilins is further complicated by the presence of multiple isoforms, which may contribute to actin dynamics by different mechanisms. We show that two isoforms, ADF and cofilin-1, are expressed in mouse NIH 3T3, B16F1, and Neuro 2A cells. Depleting cofilin-1 and/or ADF by siRNA leads to an accumulation of F-actin and to an increase in cell size. Cofilin-1 and ADF seem to play overlapping roles in cells, because the knockdown phenotype of either protein could be rescued by overexpression of the other one. Cofilin-1 and ADF knockdown cells also had defects in cell motility and cytokinesis, and these defects were most pronounced when both ADF and cofilin-1 were depleted. Fluorescence recovery after photobleaching analysis and studies with an actin monomer-sequestering drug, latrunculin-A, demonstrated that these phenotypes arose from diminished actin filament depolymerization rates. These data suggest that mammalian ADF and cofilin-1 promote cytoskeletal dynamics by depolymerizing actin filaments and that this activity is critical for several processes such as cytokinesis and cell motility.
    MeSH term(s) Actins/drug effects ; Actins/genetics ; Actins/metabolism ; Animals ; Blotting, Western ; Bridged Bicyclo Compounds, Heterocyclic/pharmacology ; Cell Line, Tumor ; Cell Movement/genetics ; Cell Size ; Cofilin 1 ; Cytokinesis/genetics ; Destrin ; Fibroblasts/metabolism ; Fibronectins/metabolism ; Fluorescein-5-isothiocyanate ; Fluorescence Recovery After Photobleaching ; Fluorescent Antibody Technique ; Fluorescent Dyes ; Gene Silencing ; Indoles ; Kinetics ; Melanoma, Experimental/metabolism ; Mice ; Microfilament Proteins/genetics ; Microfilament Proteins/metabolism ; Microscopy, Video ; NIH 3T3 Cells ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA, Small Interfering/metabolism ; Stress Fibers/metabolism ; Thiazoles/pharmacology ; Thiazolidines
    Chemical Substances Actins ; Bridged Bicyclo Compounds, Heterocyclic ; Cfl1 protein, mouse ; Cofilin 1 ; Destrin ; Dstn protein, mouse ; Fibronectins ; Fluorescent Dyes ; Indoles ; Microfilament Proteins ; Protein Isoforms ; RNA, Small Interfering ; Thiazoles ; Thiazolidines ; DAPI (47165-04-8) ; Fluorescein-5-isothiocyanate (I223NX31W9) ; latrunculin A (SRQ9WWM084)
    Language English
    Publishing date 2005-02
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E04-07-0555
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 410: Show issues

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