A gene for speed?: The evolution and function of α-actinin-3

被引：183

作者：

MacArthur, DG ^{[1
]}

North, KN ^{[1
]}

机构：

[1] Childrens Hosp, Westmead, NSW 2145, Australia

来源：

BIOESSAYS | 2004年 / 26卷 / 07期

关键词：

D O I：

10.1002/bies.20061

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The alpha-actinins are an ancient family of actin-binding proteins that play structural and regulatory roles in cytoskeletal organisation and muscle contraction. alpha-actinin-3 is the most-highly specialised of the four mammalian alpha-actinins, with its expression restricted largely to fast glycolytic fibres in skeletal muscle. Intriguingly, a significant proportion (similar to18%) of the human population is totally deficient in alpha-actinin-3 due to homozygosity for a premature stop codon polymorphism (R577X) in the ACTN3gene. Recent work in our laboratory has revealed a strong association between R577X genotype and performance in a variety of athletic endeavours. We are currently exploring the function and evolutionary history of the ACTN3 gene and other alpha-actinin family members. The alpha-actinin family provides a fascinating case study in molecular evolution, illustrating phenomena such as functional redundancy in duplicate genes, the evolution of protein function, and the action of natural selection during recent human evolution. (C) 2004 Wiley Periodicals, Inc.

引用

收藏

页码：786 / 795

页数：10

相关论文

共 68 条

[1] PRIMARY STRUCTURE OF CHICKEN SKELETAL-MUSCLE AND FIBROBLAST ALPHA-ACTININS DEDUCED FROM CDNA SEQUENCES [J].

ARIMURA, C ;

SUZUKI, T ;

YANAGISAWA, M ;

IMAMURA, M ;

HAMADA, Y ;

MASAKI, T .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 177 (03) :649-655

[2] CLONING, SEQUENCING, AND MAPPING OF AN ALPHA-ACTININ GENE FROM THE NEMATODE CAENORHABDITIS-ELEGANS [J].

BARSTEAD, RJ ;

KLEIMAN, L ;

WATERSTON, RH .

CELL MOTILITY AND THE CYTOSKELETON, 1991, 20 (01) :69-78

[3]

BEGGS AH, 1992, J BIOL CHEM, V267, P9281

[4] THE STRUCTURE AND FUNCTION OF ALPHA-ACTININ [J].

BLANCHARD, A ;

OHANIAN, V ;

CRITCHLEY, D .

JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY, 1989, 10 (04) :280-289

[5] Evidence for an uncommon α-actinin protein in Trichomonas vaginalis [J].

Bricheux, G ;

Coffe, G ;

Pradel, N ;

Brugerolle, G .

MOLECULAR AND BIOCHEMICAL PARASITOLOGY, 1998, 95 (02) :241-249

[6] The adenosine A2A receptor interacts with the actin-binding protein α-actinin [J].

Burgueño, J ;

Blake, DJ ;

Benson, MA ;

Tinsley, CL ;

Esapa, CT ;

Canela, EI ;

Penela, P ;

Mallol, J ;

Mayro, F ;

Lluis, C ;

Franco, R ;

Ciruela, F .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (39) :37545-37552

[7] Human skeletal muscle-specific α-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo [J].

Chan, YM ;

Tong, HQ ;

Beggs, AH ;

Kunkel, LM .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1998, 248 (01) :134-139

[8] A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber type [J].

Chin, ER ;

Olson, EN ;

Richardson, JA ;

Yano, Q ;

Humphries, C ;

Shelton, JM ;

Wu, H ;

Zhu, WG ;

Bassel-Duby, R ;

Williams, RS .

GENES & DEVELOPMENT, 1998, 12 (16) :2499-2509

[9] Amorphin is phosphorylase; Phosphorylase is an alpha-actinin-binding protein [J].

Chowrashi, P ;

Mittal, B ;

Sanger, JM ;

Sanger, JW .

CELL MOTILITY AND THE CYTOSKELETON, 2002, 53 (02) :125-135

[10] A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of α-actinin-2 [J].

Cukovic, D ;

Lu, GWK ;

Wible, B ;

Steele, DF ;

Fedida, D .

FEBS LETTERS, 2001, 498 (01) :87-92

← 1 2 3 4 5 6 7 →