Biochemical Characterization of the L-Plastin−Actin Interaction Shows a Resemblance with That of α-Actinin and Allows a Distinction To Be Made between the Two Actin-Binding Domains of the Molecule-Reference-Cited by-同舟云学术

Biochemical Characterization of the L-Plastin−Actin Interaction Shows a Resemblance with That of α-Actinin and Allows a Distinction To Be Made between the Two Actin-Binding Domains of the Molecule

Published:2004-02-10 Issue:9 Volume:43 Page:2428-2437
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lebart M.-C.¹,Hubert F.¹,Boiteau C.¹,Ventéo S.¹,Roustan C.¹,Benyamin Y.¹

Affiliation:

1. UMR 5539, Laboratoire de Motilité Cellulaire (EPHE), USTL, Bât.24, 4ème étage, cc 107, place E. Bataillon, 34095 Montpellier, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi030151p

Reference59 articles.

1. Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins.

2. Daudet, N., and Lebart, M.C. (2002) Transient expression of the T-isoform of plastin/fimbrin in the stereocilia of developing auditory hair cells,Cell Motil. Cytoskeleton53, 326−336.

3. Cytoskeletal differences between stereocilia of the human sperm passageway and microvilli/stereocilia in other locations

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