An F-actin binding protein in vertebrate cells that cross-links actin filaments into regular parallel arrays. It is found in both the Z line and the I band of striated muscle.
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This complex consists of alpha-actinin and talin which bind to the cytoplasmic C-terminal tail of the integrin and paxillin and vinculin which bind to talin and alphctinin.
In this regard, one of the genes that may influence these phenotypes is the alpha-actinin 3 (ACTN3) gene (Clarkson et al.
1992) Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11.
2009) Human angiotensin-converting enzyme I/D and alpha-actinin 3 R577X genotypes and muscle functional and contractile properties.
1996) Deficiency of a skeletal muscle isoform of alpha-actinin (alpha-actinin-3) in merosin-positive congenital muscular dystrophy.
The effect of alpha-actinin 3 (ACTN3) and angiotensin-converting enzyme (ACE) on endurance or sprint athletic performance have been documented.
A protein called vinculin moves cylinder-like fingers to form a hand to which an arm extended by a protein partner called alpha-actinin can bind
The images show how a protein called alpha-actinin partly unravels its structure to free an internal molecular "arm" that reaches out to another protein, called vinculin.
The researchers used a technique called X-ray crystallography to create these images, which help explain how alpha-actinin recruits vinculin to help it brace the cell's skeleton during the physically stressful process of cell movement.
Along the edge of the skeleton, near the cell membrane, the alpha-actinin molecules do double duty.
Alpha-actinin molecules bound to the skeleton also bind to the end of integrin that is inside the cell.
In the cell, that sort of stress could destroy the link between alpha-actinin and actin molecules and destabilize the cell's skeleton.