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A more recent version of this article appeared on June 1, 2003
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Submitted on July 30, 2002
Revised on December 1, 2002
Accepted on December 19, 2002
1 Department of Cell Biology and Human Anatomy, University of California, Davis
* Corresponding author. E-mail address: kabeck{at}ucdavis.edu.
We have previously identified a Golgi-localized spectrin isoform using an antibody to the 
-subunit of erythrocyte spectrin (Beck et al., 1994, J. Cell Biol., 127). In this study we show that a screen of a 
gt11 expression library resulted in the isolation of a ~5 kb partial cDNA from a Madin Darby bovine kidney cell line (MDBK) which encoded a polypeptide of 1697 amino acids with low, but detectable, sequence homology to spectrin (37%). A blast search revealed that this clone overlaps with the 5' end of a recently identified spectrin family member Syne-1B/Nesprin-1, an alternately transcribed gene with muscle-specific forms that bind acetylcholine receptor and associate with the nuclear envelope (Apel et al. 2000, J. Biol. Chem., 257; Zang et al., 2001, J. Cell Sci., 114). By comparing the sequence of the MDBK clone with sequence data from the human genome database, we have determined that this cDNA represents a central portion of a very large gene (~500 kb), encoding a ~25 kb transcript that we refer to as Syne-1. Syne-1 encodes a large polypeptide (8406 amino acids) with multiple spectrin repeats and a region at its amino terminus with high homology to the actin binding domains of conventional spectrins. Golgi-localization for this spectrin-like protein was demonstrated by expression of epitope-tagged fragments in MDBK and COS cells, identifying two distinct Golgi binding sites, and by immunofluorescence microscopy using several different antibody preparations. One of the Golgi binding domains on Syne-1 acts as a dominant negative inhibitor that alters the structure of the Golgi complex, which collapses into a condensed structure near the centrosome in transfected epithelial cells. We conclude that the Syne-1 gene is expressed in a variety of forms that are multifunctional and are capable of functioning at both the Golgi and the nuclear envelope, perhaps linking the two organelles during muscle differentiation.
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