Literature DB >> 2203335

The functional importance of multiple actin isoforms.

P A Rubenstein1.   

Abstract

Actin is a protein that plays an important role in cell structure, cell motility, and the generation of contractile force in both muscle and nonmuscle cells. In many organisms, multiple forms of actin, or isoactins, are found. These are products of different genes and have different, although very similar, amino acid sequences. Furthermore, these isoactins are expressed in a tissue specific fashion that is conserved across species, suggesting that their presence is functionally important and their behavior can be distinguished quantitatively from one another in vitro. In muscle cells, they are differentially distributed within the cell and some are specifically associated with structures such as costameres, mitochondria, and neuromuscular junctions. There is also good evidence for specific isoactin function in microvascular pericytes and in the intestinal brush border. However, the necessity of specific isoactins for various functions has not yet been conclusively demonstrated.

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Year:  1990        PMID: 2203335     DOI: 10.1002/bies.950120702

Source DB:  PubMed          Journal:  Bioessays        ISSN: 0265-9247            Impact factor:   4.345


  68 in total

Review 1.  Isovariant dynamics expand and buffer the responses of complex systems: the diverse plant actin gene family.

Authors:  R B Meagher; E C McKinney; M K Kandasamy
Journal:  Plant Cell       Date:  1999-06       Impact factor: 11.277

2.  Smooth muscle α actin is specifically required for the maintenance of lactation.

Authors:  Nate Weymouth; Zengdun Shi; Don C Rockey
Journal:  Dev Biol       Date:  2011-11-12       Impact factor: 3.582

3.  One plant actin isovariant, ACT7, is induced by auxin and required for normal callus formation.

Authors:  M K Kandasamy; L U Gilliland; E C McKinney; R B Meagher
Journal:  Plant Cell       Date:  2001-07       Impact factor: 11.277

4.  The sarcoplasmic reticulum: Actin and tropomodulin hit the links.

Authors:  David S Gokhin; Velia M Fowler
Journal:  Bioarchitecture       Date:  2011-07-01

5.  Isolation, characterization, and expression analysis of three actin genes in the New Zealand black-footed abalone, Haliotis iris.

Authors:  Maxine J Bryant; Heather J Flint; Frank Y T Sin
Journal:  Mar Biotechnol (NY)       Date:  2006-01-01       Impact factor: 3.619

6.  Differential regulation of actin polymerization and structure by yeast formin isoforms.

Authors:  Kuo-Kuang Wen; Peter A Rubenstein
Journal:  J Biol Chem       Date:  2009-04-22       Impact factor: 5.157

7.  Importance of a Lys113-Glu195 intermonomer ionic bond in F-actin stabilization and regulation by yeast formins Bni1p and Bnr1p.

Authors:  Kuo-Kuang Wen; Melissa McKane; Peter A Rubenstein
Journal:  J Biol Chem       Date:  2013-05-07       Impact factor: 5.157

8.  Actin Purified from Maize Pollen Functions in Living Plant Cells.

Authors:  H. Ren; B. C. Gibbon; S. L. Ashworth; D. M. Sherman; M. Yuan; C. J. Staiger
Journal:  Plant Cell       Date:  1997-08       Impact factor: 11.277

9.  Alterations in the expression of the beta-cytoplasmic and the gamma-smooth muscle actins in hypertrophied urinary bladder smooth muscle.

Authors:  Y S Kim; Z Wang; R M Levin; S Chacko
Journal:  Mol Cell Biochem       Date:  1994-02-23       Impact factor: 3.396

10.  Molecular analysis of an actin gene, CarACT1, from chickpea (Cicer arietinum L.).

Authors:  Hui Peng; Huiying Cheng; Xingwang Yu; Qinghua Shi; Hua Zhang; Jiangui Li; Hao Ma
Journal:  Mol Biol Rep       Date:  2010-02       Impact factor: 2.316

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