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LMW-PTP associates and dephosphorylates STAT5 interacting with its C-terminal domain

Authors
  • Rigacci, Stefania
  • Talini, Doriana
  • Berti, Andrea
Type
Published Article
Journal
Biochemical and Biophysical Research Communications
Publication Date
Jan 01, 2003
Volume
312
Issue
2
Pages
360–366
Identifiers
DOI: 10.1016/j.bbrc.2003.10.126
Source
Elsevier
Keywords
License
Unknown

Abstract

Hematopoietic cells, particularly megakaryoblastic ones, display a high level of low M r phosphotyrosine protein phosphatase (LMW-PTP) expression; nevertheless, the role of this PTP in such cellular lineages has been scarcely investigated. Here, we demonstrate that LMW-PTP is able to associate and dephosphorylate signal transducer and activator of transcription-5 (STAT5) in DAMI megakaryocytic cells. Numerous researchers repeatedly hypothesized the association of a regulatory phosphotyrosine protein phosphatase with STAT5 C-terminus, but such phosphotyrosine protein phosphatase remained unknown. We show evidence indicating that the association of STAT5 and LMW-PTP does not exclusively involve the phosphatase active site and phosphotyrosine residue of STAT5, and we individuate an essential region of interaction at STAT5 C-terminus, coinciding with the previously hypothesized PTP-associating domain.

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