Differential activities in adhesion and neurite growth of fibronectin type III repeats in the PTP-δ extracellular domain

Manuel R. Gonzalez-Brito, John L. Bixby

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

The full-length extracellular domain (ECD) of protein tyrosine phosphatase δ (PTP-δ) functions as a ligand to promote cell adhesion and neurite outgrowth; this ECD contains three immunoglobulin (Ig) repeats and eight fibronectin type III (FN III) repeats. However, it is not known which regions of the ECD regulate its ligand functions. Therefore, we constructed and expressed a fusion protein of the PTP-δ ECD lacking FN III repeats 4-8, and tested this protein for neuronal adhesion and neurite-promoting ability. Compared to the full-length isoform, the truncated ECD was poorer at promoting adhesion, but a more potent promoter of neurite growth. The results suggest that distal FN III repeats of PTP-δ are important in adhesive functions, but dispensable for neurite outgrowth promotion. As the predominant isoform of PTP-δ during neural development (type D) also lacks distal FN III repeats, the functional properties we observe may be relevant to periods of axon extension, suggesting that splice variants of receptor PTPs play distinct roles in neural development.

Original languageEnglish (US)
Pages (from-to)425-429
Number of pages5
JournalInternational Journal of Developmental Neuroscience
Volume24
Issue number7
DOIs
StatePublished - Nov 2006

Keywords

  • Axon growth
  • Cell adhesion molecule
  • Fibronectin type III repeat
  • Immunoglobulin domain
  • Protein tyrosine phosphatase

ASJC Scopus subject areas

  • Developmental Biology
  • Developmental Neuroscience

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