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Originally published In Press as doi:10.1074/mcp.M800394-MCP200 on January 30, 2009.
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Molecular & Cellular Proteomics 8:1295-1305, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

The Organelle Proteome of the DT40 Lymphocyte Cell Line*,Formula

Stephanie L. Hall{ddagger}, Svenja Hester§, Julian L. Griffin{ddagger}, Kathryn S. Lilley§ and Antony P. Jackson{ddagger},¶

From the {ddagger}Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, United Kingdom and
§Cambridge Centre for Proteomics, Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QW, United Kingdom

A major challenge in eukaryotic cell biology is to understand the roles of individual proteins and the subcellular compartments in which they reside. Here, we use the localization of organelle proteins by isotope tagging technique to complete the first proteomic analysis of the major organelles of the DT40 lymphocyte cell line. This cell line is emerging as an important research tool because of the ease with which gene knockouts can be generated. We identify 1090 proteins through the analysis of preparations enriched for integral membrane or soluble and peripherally associated proteins and localize 223 proteins to the endoplasmic reticulum, Golgi, lysosome, mitochondrion, or plasma membrane by matching their density gradient distributions to those of known organelle residents. A striking finding is that within the secretory and endocytic pathway a high proportion of proteins are not uniquely localized to a single organelle, emphasizing the dynamic steady-state nature of intracellular compartments in eukaryotic cells.

¶ To whom correspondence should be addressed: Tel.: 44-1223-765951; Fax:44-1223-333345; E-mail: apj10{at}bioc.cam.ac.uk


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