Functional nature of a novel mutant CYLD observed in pediatric lymphoblastic B-cell leukemia

Pediatr Blood Cancer. 2015 Jun;62(6):1066-9. doi: 10.1002/pbc.25387. Epub 2015 Jan 16.

Abstract

The Deubiquitinating enzyme, Cylindromatosis (CYLD), has been established as a crucial regulator of B-cells. The present study was addressed to identify the nature of CYLD-dependent RNomics in patients of pediatric age group with B-ALL. The study revealed the presence of a novel mutant CYLD of 55 kDa in these patients. The mutant CYLD displayed its ability to restrict the cells in G2 phase of cell cycle, down-regulate PLK-1 and block the nuclear translocation of BCL3. Based upon these results, we propose that this mutant CYLD has the capacity to act as a differential marker characteristic of B-cell lymphoblastic leukemia. Pediatr Blood Cancer 2015;62:1066-1069. © 2015 Wiley Periodicals, Inc.

Keywords: BCL3; CYLD; PLK-1; human PBMCs; pediatric B-ALL.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Child
  • Deubiquitinating Enzyme CYLD
  • Humans
  • Leukemia, B-Cell / enzymology
  • Leukemia, B-Cell / genetics*
  • Mutation*
  • Precursor Cell Lymphoblastic Leukemia-Lymphoma / enzymology
  • Precursor Cell Lymphoblastic Leukemia-Lymphoma / genetics*
  • Tumor Suppressor Proteins / genetics*

Substances

  • Tumor Suppressor Proteins
  • CYLD protein, human
  • Deubiquitinating Enzyme CYLD