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Original Research Open Access

A Newly Characterized, Two BRCT Domain-Containing Isoform of PAX-Interacting Protein (PTIP) Generated via Frame Shift and Alternative Pre-mRNA Splicing

  • 1Department of Biology, Arts and Sciences, New York University in Shanghai, Shanghai 200122, China
  • 2Molecular Biosciences, University of Texas at Austin, 1 University Station A5000, Austin, TX 78712, USA
  • 3Department of Molecular Science and Technology, Advanced College of Bio-Convergence Engineering, Ajou University 206 Worldcup-ro, Yeongtong-gu, Suwon 16499, South Korea
+ Affiliations - Affiliations

Corresponding Author

Haley O. Tucker, haleytucker@austin.utexas.edu

Received Date: October 13, 2025

Accepted Date: November 28, 2025

Abstract

In an effort to clone polyglutamine-rich factors from activated B lymphocytes of mice, we discovered and describe here a previously uncharacterized isoform of PTIP/PAXIP1. By virtue of a two-nucleotide frameshift followed by alternative pre-mRNA splicing, this shorter isoform of 576 amino acids (termed PTIP576) retained only the two central BRCT domains of previously characterized PTIP and encodes a unique and structurally disordered 50 residue C-terminus. PTIP576 is expressed primarily in nuclei of progenitor and activated mature B lymphocytes. Transgenic overexpression of PTIP576 in murine B and T cells led to increased lineages of bone marrow B cells and thymocyte CD4 T cells. We conclude by addressing potential functions of PTIP576 resulting from the relatively unique mechanism by which it is engendered.

Keywords

B cells, Breast cancer C-Terminal, Lymphocytes, Plasma cells

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