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Luo, R.T., Lavau, C., Du, C.C., Simone, F., Polak, P.E., Kawamata, S. and Thirman, M.J. (2001) The elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELLinduced leukemogenesis. Molecular and Cellular Biology, 21, 5678-5687. doi:10.1128/MCB.21.16.5678-5687.2001

has been cited by the following article:

• TITLE: Shared and discrete interacting partners of ELL1 and ELL2 by yeast two-hybrid assay

  AUTHORS: Fortuna Arumemi, Ian Bayles, Joshua Paul, Christine Milcarek

  KEYWORDS: Transcription Elongation; Immunoglobulin Synthesis; Yeast Two-Hybrid System

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.7, July 3, 2013

  ABSTRACT: ELL2 (eleven-nineteen lysine-rich leukemia transcription elongation factor), a component of a larger complex with pTEFb (cyclin T and CDK9) and AF4, is up-regulated in plasma cells where it influences mRNA processing by increasing exon skipping and enhancing proximal poly (A) site use. ELL2 is needed to produce the secretory-specific Ig heavy chain mRNA while ELL1 mRNA does not change in abundance with B cell stages. To investigate the potential interactions of other proteins with the ELL1 and ELL2 proteins, we preformed yeast two-hybrid studies. HSP40 and Testin were found to bind to ELL2 in its amino-terminal half. PCNA binds to ELL2 in a region encompassing amino acids 186 - 344. The potent transcription factors HIF1 α and ZNF622 interact with both ELL1 and 2 in the central, proline rich region. Meanwhile, BBS2 and ING3 interact with ELL1 but not ELL2 in this central proline-rich region. Many of the ELL-interacting-proteins uncovered in the two-hybrid screen are tumour suppressors that may work through the ELL: pTEFb complex to suppress or activate sets of genes in plasma cells.