Serine palmitoyltransferase subunit 1 is present in the endoplasmic reticulum,nucleus and focal adhesions,and functions in cell morphology |
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| Authors: | Jia Wei Tokunbo Yerokun Martina Leipelt Chris A Haynes Harish Radhakrishna Amin Momin Samuel Kelly Hyejung Park Elaine Wang Jill M Carton David J Uhlinger Alfred H Merrill Jr |
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| Institution: | 1. School of Biology and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332, USA;2. The Coca-Cola Company, P.O. Box 1734, Atlanta, GA 30301, USA;3. Department of Molecular and Cellular Biology, Centocor, Inc., Malvern, PA, USA;4. Drug Discovery, Johnson and Johnson Pharmaceutical Research and Development, Raritan, NJ 08869, USA |
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| Abstract: | Serine palmitoyltransferase (SPT) has been localized to the endoplasmic reticulum (ER) by subcellular fractionation and enzymatic assays, and fluorescence microscopy of epitope-tagged SPT; however, our studies have suggested that SPT subunit 1 might be present also in focal adhesions and the nucleus. These additional locations have been confirmed by confocal microscopy using HEK293 and HeLa cells, and for focal adhesions by the demonstration that SPT1 co-immunoprecipitates with vinculin, a focal adhesion marker protein. The focal adhesion localization of SPT1 is associated with cell morphology, and possibly cell migration, because it is seen in most cells before they reach confluence but disappears when they become confluent, and is restored by a standard scratch-wound healing assay. Conversely, elimination of SPT1 using SPTLC1 siRNA causes cell rounding. Thus, in addition to its “traditional” localization in the ER for de novo sphingolipid biosynthesis, SPT1 is present in other cellular compartments, including focal adhesions where it is associated with cell morphology. |
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| Keywords: | Sphingolipid metabolizing enzyme Subcellular localization Focal adhesion |
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