The novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation.

A novel cytoplasmic protein-tyrosine phosphatase (PTPase) designated PTP20 was isolated from a PC12 cDNA library and shown to positively regulate the differentiation process in PC12 cells. The PTP20 open reading frame of 453 amino acids contains a single tyrosine phosphatase catalytic domain and displays closest homology to members of the PTP-PEST protein-tyrosine phosphatase family. Transient expression of PTP20 in Rat-1 cells resulted in the expression of a 50-kDa protein which exhibited PTPase activity in vitro. Expression of the 2.3-kilobase PTP20 mRNA increased during differentiation of nerve growth factor (NGF)-stimulated PC12 cells. Consistent with this observation, stable overexpression of PTP20 in PC12 cells resulted in accelerated neurite formation following NGF treatment. These findings suggest a positive regulatory role of PTP20 in NGF-dependent neuronal differentiation of PC12 cells.

• Publication year

  2010

• Venue

  Journal of Biological Chemistry

• Publication date

  2010-10-15

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1074/jbc.a110.029422PMID 8910608
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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