Literature DB >> 8689567

Control of actin assembly at filament ends.

D A Schafer1, J A Cooper.   

Abstract

Actin filament polymerization involves exchange of subunits of filament ends, which can be controlled in vitro and in vivo by other proteins that bind actin filaments and inhibit subunit addition or loss at the ends. Proteins that bind to the barbed end, including capping protein, the gelsolin super-family, tensin, and profilin are discussed, as are proteins that bind to the pointed end, including tropomodulin and spectrin/band 4.1. Some proteins that bind along the sides of filaments and influence assembly at ends are also discussed. Functional roles in vivo are emphasized.

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Year:  1995        PMID: 8689567     DOI: 10.1146/annurev.cb.11.110195.002433

Source DB:  PubMed          Journal:  Annu Rev Cell Dev Biol        ISSN: 1081-0706            Impact factor:   13.827


  54 in total

1.  Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments.

Authors:  O Poupel; H Boleti; S Axisa; E Couture-Tosi; I Tardieux
Journal:  Mol Biol Cell       Date:  2000-01       Impact factor: 4.138

Review 2.  Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms.

Authors:  A Weber
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

Review 3.  Actin and pollen tube growth.

Authors:  L Vidali; P K Hepler
Journal:  Protoplasma       Date:  2001       Impact factor: 3.356

Review 4.  Cytoplasmic dynein and microtubule transport in the axon: the action connection.

Authors:  K K Pfister
Journal:  Mol Neurobiol       Date:  1999 Oct-Dec       Impact factor: 5.590

5.  Crystal structure of CapZ: structural basis for actin filament barbed end capping.

Authors:  Atsuko Yamashita; Kayo Maeda; Yuichiro Maéda
Journal:  EMBO J       Date:  2003-04-01       Impact factor: 11.598

6.  Regulation of sodium channel activity by capping of actin filaments.

Authors:  Ekaterina V Shumilina; Yuri A Negulyaev; Elena A Morachevskaya; Horst Hinssen; Sofia Yu Khaitlina
Journal:  Mol Biol Cell       Date:  2003-04       Impact factor: 4.138

7.  Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function.

Authors:  Alessia Di Nardo; Gregor Cicchetti; Hervé Falet; John H Hartwig; Thomas P Stossel; David J Kwiatkowski
Journal:  Proc Natl Acad Sci U S A       Date:  2005-10-27       Impact factor: 11.205

Review 8.  Structural genomics of protein phosphatases.

Authors:  Steven C Almo; Jeffrey B Bonanno; J Michael Sauder; Spencer Emtage; Teresa P Dilorenzo; Vladimir Malashkevich; Steven R Wasserman; S Swaminathan; Subramaniam Eswaramoorthy; Rakhi Agarwal; Desigan Kumaran; Mahendra Madegowda; Sugadev Ragumani; Yury Patskovsky; Johnjeff Alvarado; Udupi A Ramagopal; Joana Faber-Barata; Mark R Chance; Andrej Sali; Andras Fiser; Zhong-yin Zhang; David S Lawrence; Stephen K Burley
Journal:  J Struct Funct Genomics       Date:  2007-12-05

9.  Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modeling.

Authors:  Eliana D Grimm; Rodrigo V Portugal; Mário de Oliveira Neto; Nádia H Martins; Igor Polikarpov; Arnaldo Zaha; Henrique B Ferreira
Journal:  Biophys J       Date:  2006-02-10       Impact factor: 4.033

10.  Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties.

Authors:  David S Gokhin; Marie-Louise Bang; Jianlin Zhang; Ju Chen; Richard L Lieber
Journal:  Am J Physiol Cell Physiol       Date:  2009-03-18       Impact factor: 4.249

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