Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase

FEBS Lett. 2003 Feb 27;537(1-3):203-9. doi: 10.1016/s0014-5793(03)00127-3.

Abstract

We have molecularly cloned TPP36, a novel 36 kDa protein with 281 amino acids that was identified as a protein phosphorylated in B progenitor cells following stimulation with pervanadate/H(2)O(2). Analysis with anti-TPP36 antiserum revealed that TPP36 was expressed ubiquitously and had an isoform with 236 amino acids, designated TPP32. TPP36/32 were localized mainly in cytoplasm despite the presence of a typical nuclear localization signal sequence. These proteins were phosphorylated preferentially by Abl among a panel of tyrosine kinases examined. Phosphorylation of tyrosine 120 in TPP36/32 led to an apparent mobility shift in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting conformational change in the phosphorylated protein. Thus, TPP36/32 appear to be novel substrates of Abl tyrosine kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cloning, Molecular
  • Humans
  • Mice
  • Molecular Sequence Data
  • Oncogene Proteins v-abl / metabolism*
  • Oryzias
  • Phosphoproteins / genetics*
  • Phosphoproteins / metabolism
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins c-abl
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Xenopus

Substances

  • Cdv3 protein, mouse
  • Oncogene Proteins v-abl
  • Phosphoproteins
  • Protein Isoforms
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins c-abl