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Science 9 August 1996:
Vol. 273. no. 5276, pp. 797 - 801
DOI: 10.1126/science.273.5276.797
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Reports

Diffusional Mobility of Golgi Proteins in Membranes of Living Cells

Nelson B. Cole, Carolyn L. Smith, Noah Sciaky, * Mark Terasaki, Michael Edidin, Jennifer Lippincott-Schwartz dagger

The mechanism by which Golgi membrane proteins are retained within the Golgi complex in the midst of a continuous flow of protein and lipid is not yet understood. The diffusional mobilities of mammalian Golgi membrane proteins fused with green fluorescent protein from Aequorea victoria were measured in living HeLa cells with the fluorescence photobleaching recovery technique. The diffusion coefficients ranged from 3 × 10-9 square centimeters per second to 5 × 10-9 square centimeters per second, with greater than 90 percent of the chimeric proteins mobile. Extensive lateral diffusion of the chimeric proteins occurred between Golgi stacks. Thus, the chimeras diffuse rapidly and freely in Golgi membranes, which suggests that Golgi targeting and retention of these molecules does not depend on protein immobilization.


[Web Site] Authors' site which includes movies

N. B. Cole, N. Sciaky, J. Lippincott-Schwartz, Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Building 18T, National Institutes of Health, Bethesda, MD 20892, USA.
C. L. Smith, National Institute of Neurological Disorders and Stroke, Building 36, National Institutes of Health, Bethesda, MD 20892, USA.
M. Terasaki, Department of Physiology, University of Connecticut Health Center, Farmington, CT 06032, USA.
M. Edidin, Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA.
*   Present address: National Jewish Center for Immunology and Respiratory Medicine, 1400 Jackson Street, Denver, CO 80206, USA.

dagger    To whom correspondence should be addressed. E-mail: jlippin{at}helix.nih.gov


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