• Assistant Project Scientist (under Prof. Timothy Baker)
  • Dept. Chemistry and Biochemistry, UCSD
  • 4107 Natural Sciences Bldg., MC-0378
  • La Jolla, CA 92093

I was a PhD student in dr. Taylor’s lab from 1995-2000. For my dissertation, I obtained a 3-D reconstructed image of skeletal muscle α-ctinin and built a pseudo atomic model.

α-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

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