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Maria Gomez

Maria Gomez

Professor

Maria Gomez

Individual domains of Tensin2 exhibit distinct subcellular localisations and migratory effects.

Author

  • Sassan Hafizi
  • Emma Sernstad
  • Jerome D Swinny
  • Maria Gomez
  • Björn Dahlbäck

Summary, in English

Tensins are large intracellular proteins believed to link the extracellular matrix to the cytoskeleton via integrins. Tensins are multidomain proteins consisting of homologous C1, PTPase, C2, SH2 and PTB domains. Full-length Tensin proteins can undergo cleavage inside cells, thus yielding domains in isolation that may have discrete subcellular localisations and downstream effects. We expressed different isoforms of Tensin2 and their individual domains as recombinant green fluorescent protein (GFP)-fusion constructs in DU145 human prostate cancer cells. Under fluorescence confocal microscopy, the isolated domains of Tensin2 all displayed discrete distributions throughout the cytoplasm and the nucleus. In particular, partial constructs containing the C1 domain localised preferentially to the nucleus, including the isolated C1 domain and the PTPase domain. In contrast, all three full-length isoforms of Tensin2 were present exclusively in discrete punctate bodies throughout the cytoplasm. This punctate staining showed colocalisation with the tumour suppressor protein DLC-1 as well as with actin (phalloidin). Furthermore, DU145 cells transiently expressing partial Tensin2 constructs containing the PTB domain showed an increased haptotactic migration. In addition, stimulation of renal carcinoma cells stably expressing Tensin2 by the survival factor Gas6 caused phosphorylation of its receptor Axl, but no effect on Tensin2, which was already maximally phosphorylated at time 0. In conclusion, our results indicate that differential proteolytic cleavage of Tensin2 can liberate domains with discrete localisations and functions, which has implications for the role of Tensins in cancer cell survival and motility.

Department/s

  • Clinical Chemistry, Malmö
  • Vascular Physiology
  • EXODIAB: Excellence in Diabetes Research in Sweden

Publishing year

2010

Language

English

Pages

52-61

Publication/Series

International Journal of Biochemistry and Cell Biology

Volume

42

Document type

Journal article

Publisher

Elsevier

Topic

  • Physiology
  • Medicinal Chemistry

Status

Published

Research group

  • Clinical Chemistry, Malmö
  • Vascular Physiology

ISBN/ISSN/Other

  • ISSN: 1878-5875