Nesprins, but not sun proteins, switch isoforms at the nuclear envelope during muscle development

K. Natalie Randles, Le Thanh Lam, Caroline A. Sewry, Megan Puckelwartz, Denis Furling, Manfred Wehnert, Elizabeth M. McNally, Glenn E. Morris

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Nesprins are a family of nuclear transmembrane proteins anchored via Sun proteins to the nuclear membrane. Analysis of nesprins during human muscle development revealed an increase in nesprin-1-giant during early myogenesis in vitro. During the transition from immature to mature muscle fibres in vivo, nesprin-2 partly replaced nesprin-1 at the nuclear envelope and short nesprin isoforms became dominant. Sun1 and Sun2 proteins remained unchanged during this fibre maturation. In emerin-negative skin fibroblasts, nesprin-2-giant was relocated from the nuclear envelope to the cytoplasm, not to the endoplasmic reticulum, while nesprin-1 remained at the nuclear envelope. In emerin-negative keratinocytes lacking nesprin-1, nesprin-2 remained at the nuclear envelope. HeLa cell nuclear envelopes lacked nesprin-1, which was the dominant form in myoblasts, while a novel 130-kD nesprin-2 isoform dominated Ntera-2 cells. The results suggest the possibility of isoform-specific and tissue-specific roles for nesprins in nuclear positioning.

Original languageEnglish (US)
Pages (from-to)998-1009
Number of pages12
JournalDevelopmental Dynamics
Volume239
Issue number3
DOIs
StatePublished - Mar 2010

Keywords

  • Emerin
  • Enaptin
  • Epitope mapping
  • Golgi
  • Lamin A/C
  • MYNE
  • Monoclonal antibody
  • Muscle development
  • Myogenesis
  • NT-2
  • NUANCE
  • Nesprin
  • Nuclear envelope
  • Nuclear lamina
  • Nuclear membrane
  • Nuclear positioning
  • Phage display
  • SYNE

ASJC Scopus subject areas

  • Developmental Biology

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