|
|
 |
 |
| |
 Printable version |
MDS1/EVI-1, a new member of PR domain protein involved in tumorigenesis |
Hématologie. Volume 8, Number 2, 121-8, Mars - Avril 2002, Revues et mini-revues
|
 Résumé
Article gratuit
|
Author(s) : Laurence Legros, Sophie Raynaud |
Summary : MDS1-EVI-1, a zinc-finger DNA-binding transcription activator, is encoded by a gene located at the 3q26 chromosomal band originally identified as two separated genes, EVI1 and MDS1. Whereas EVI1 expression is not found in adult human and mouse hematopoietic cells, both genes were first detected, in humans, in leukemic myeloid cells with 3q26 rearrangements such as t(3;3)(q21;q26) and inv(3)(q21q26) leading to overexpression of EVI1, or t(3;21)(q26;q22) and t(3;12)(q26;p13) resulting in MDS1 alterations. MDS1-EVI1 encodes a PR domain, a protein motif suggested to have an inhibiting role in tumorigenesis, that characterizes a subfamily of Krüppel-like zinc finger genes whose members, such as the retinoblastoma-binding protein RIZ and the transcription repressor PRD1-BF1/Blimp-1, are thought to play an important role in cell differentiation and malignant transformation. The founding member of this family, the RIZ gene, isolated because of its product binding to the retinoblastoma tumor suppressor protein, encodes two proteins named RIZ1 and RIZ2, the RIZ2 product lacking the NH2-terminal PR domain of RIZ1. Similarly, EVI1 is now considered as a PR-domain lacking product of the MDS1-EVI1 gene initiated from an internal promoter. Such aberrant truncated forms of MDS1-EVI1 are generated through 3q26 rearrangements, leading to major changes of its transcriptional properties and to leukemic transformation of the rearranged cells. |
Keywords : MDS1/EVI-1, leukemia, myelodysplastic syndrome. |
|
