Identification and characterization of GSRP-56, a novel Golgi-localized spectrin repeat-containing protein

Yuko Kobayashi, Yuki Katanosaka, Yuko Iwata, Masayuki Matsuoka, Munekazu Shigekawa, Shigeo Wakabayashi

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


Spectrin repeat (SR)-containing proteins are important for regulation of integrity of biomembranes, not only the plasma membrane but also those of intracellular organelles, such as the Golgi, nucleus, endo/lysosomes, and synaptic vesicles. We identified a novel SR-containing protein, named GSRP-56 (Golgi-localized SR-containing protein-56), by a yeast two-hybrid method, using a member of the transient receptor potential channel family, TRPV2, as bait. GSRP-56 is an isoform derived from a giant SR-containing protein, Syne-1 (synaptic nuclear envelope protein-1, also referred to as Nesprin-1 or Enaptin), predicted to be produced by alternative splicing. Immunological analysis demonstrated that this isoform is a 56-kDa protein, which is localized predominantly in the Golgi apparatus in cardiomyocytes and C2C12 myoblasts/myotubes, and we found that two SR domains were required both for Golgi targeting and for interaction with TRPV2. Interestingly, overexpression of GSRP-56 resulted in a morphological change in the Golgi structure, characterized by its enlargement of cis-Golgi marker antibody-staining area, which would result partly from fragmentation of Golgi membranes. Our findings indicate that GSRP-56 is a novel, particularly small Golgi-localized member of the spectrin family, which possibly play a role in maintenance of the Golgi structure.

Original languageEnglish
Pages (from-to)3152-3164
Number of pages13
JournalExperimental Cell Research
Issue number16
Publication statusPublished - Oct 1 2006
Externally publishedYes


  • Golgi apparatus
  • Nesprin-1
  • Spectrin repeat
  • Subcellular localization
  • Syne-1

ASJC Scopus subject areas

  • Cell Biology


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