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Related Experiment Videos

Golgi localization of Syne-1.

Lisa Lucio Gough1, Jun Fan, Stephen Chu

  • 1Department of Cell Biology and Human Anatomy, University of California, Davis, 95616, USA.

Molecular Biology of the Cell
|June 17, 2003
PubMed
Summary

Researchers identified Syne-1, a novel spectrin-like protein, localizing to the Golgi apparatus. This protein impacts Golgi structure and may link the Golgi and nuclear envelope during muscle development.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Previously identified a Golgi-localized spectrin isoform using antibodies to erythrocyte spectrin beta-subunit.
  • Spectrin family members, like Nesprin-1beta, are known to associate with the nuclear envelope and bind acetylcholine receptors.

Purpose of the Study:

  • To characterize a novel spectrin-like protein identified in Madin-Darby bovine kidney (MDBK) cells.
  • To determine the function and localization of this protein, named Syne-1.

Main Methods:

  • Screened a lambda gt11 expression library to isolate a partial cDNA.
  • Performed BLAST searches and compared sequences with the human genome database.
  • Expressed epitope-tagged Syne-1 fragments in MDBK and COS cells.
  • Utilized immunofluorescence microscopy with various antibodies.

Main Results:

  • Isolated a 5-kb partial cDNA encoding a 1697-amino acid polypeptide with 37% homology to spectrin.
  • Identified this cDNA as a central portion of the Syne-1 gene, a large gene (approx. 500 kb) encoding a 25-kb transcript and an 8406-amino acid polypeptide.
  • Demonstrated Golgi localization of Syne-1, identifying two distinct Golgi binding sites.
  • Showed that a Syne-1 Golgi binding domain acts as a dominant-negative inhibitor, causing Golgi collapse near the centrosome in transfected cells.

Conclusions:

  • The Syne-1 gene is expressed in multiple forms with dual localization at the Golgi and nuclear envelope.
  • Syne-1 is multifunctional and may play a role in linking the Golgi and nuclear envelope during muscle differentiation.

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