Spectrins and the Golgi

Kenneth A Beck

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


Several isoforms of spectrin membrane skeleton proteins have been localized to the Golgi complex. Golgi-specific membrane skeleton proteins associate with the Golgi as a detergent-resistant cytoskeletal structure that likely undergoes a dynamic assembly process that accommodates Golgi membrane dynamics. This review discusses the potential roles for this molecule in Golgi functions. In particular, it will focus on a recently identified distant cousin to conventional erythroid spectrin variously named Syne-1, Nesprin, myne, Enaptin, MSP-300, and Ank-1. Syne-1 has the novel ability to bind to both the Golgi and the nuclear envelope, a property that raises several intriguing and novel insights into Golgi structure and function. These include (1) the facilitation of interactions between Golgi and transitional ER sites on the nuclear envelope of muscle cells, and (2) an ability to impart localized specificity to the secretory pathway within large multinucleate syncytia such as skeletal muscle fibers.

Original languageEnglish (US)
Pages (from-to)374-382
Number of pages9
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Issue number3 SPEC. ISS.
StatePublished - Jul 10 2005


  • Golgi
  • Neuromuscular junction
  • Nuclear envelope
  • Spectrin
  • Syncytium
  • Syne-1
  • Transitional ER

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Biophysics


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