Jinghua Tang
- Department of Molecular Biology
- The Scripps Research Institute
- 10550 North Torrey Pines Road
- La Jolla, CA 92037
- phone: (858) 784-8647
- Current webpage
Alpha-actinin is an F-actin binding and cross-linking protein. It is an antiparallel
homodimer, with a subunit molecular weight of 94-103 KD. It is visualized
as a long rod-shaped molecule in the electron microscope, 3-4 nm wide and
30-40 nm in length. Alpha-actinin is a structural protein, so its physiological
importance lies in what it interacts with and where. The F-actin cross-linking
activity is its best known physiological role. It also mediates linkages between
plasma membrane and cytoskeleton. Alpha-actinin is found in a wide variety
of cells. The best known subcellular location is the Z-disk of striated muscle
where it crosslinks antiparallel actin filaments to form the I-band. In smooth
muscle, alpha-actinin is found in both cytoplasmic dense bodies and membrane
associated adhesion plaques. In non-muscle cells, alpha-actinin appears in
stress fibers and focal adhesions. It has been shown to associate with spectrin,
nebulin and tropomyosin, ICAM-1, L-selectin and beta1- and beta2-integrins
and talin, vinculin, and zyxin. Alpha-actinin is also linked to the phospholipid
signal pathways by its interactions with phosphatidylinositol 4,5-biphosphate
and phosphoinositide 3-kinase.
Recent Publications
- Tang Jinghua, Taylor, Dianne W. and Taylor, Kenneth A. The
3-D structure of a-actinin obtained by cryoelectron microscopy suggests
a model for Ca2+ dependent actin binding. J. Mol. Biol. 310(4), 845-858
(2001)
- Kenneth A. Taylor, Jinghua Tang, Yifan Cheng & Hanspeter Winkler. The use of electron tomography for structural analysis of disordered protein arrays. J. Struct. Biol. 120, 372-386 (1997)