Disease relevance of SNF8

• EAP30 is part of a transcription factor complex associated with acute myeloid leukemia, so these results may have relevance to human cancer [1].

High impact information on SNF8

• Remarkably, EAP30 can interact with ELL and derepress ELL's inhibitory activity in vitro [2].
• Cloning and characterization of the EAP30 subunit of the ELL complex that confers derepression of transcription by RNA polymerase II [2].
• Here, we report that the three subunits of human ESCRT-II, EAP20, EAP30, and EAP45, have a number of properties in common with their yeast orthologs [3].
• RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment [4].
• Residues in two amino-terminal PPXY motifs (motif I and II), involved in dimerization of Vps25p and interaction with Vps22p and Vps36p, were closely, but not absolutely conserved [5].

Biological context of SNF8

• Our findings, therefore, uncover meiosis-specific regulation of SPB maturation and provide evidence that a member of the conserved EAP30 family is required for maintenance of genome stability through regulation of SPB maturation [1].

Anatomical context of SNF8

• Here we report that the fission yeast homolog of the human transcription factor EAP30, Dot2, negatively regulates meiotic spindle pole body (SPB, the yeast equivalent of centrosome) maturation. dot2 mutants show excess electron-dense material accumulating near SPBs, which we refer to as aberrant microtubule organization centers (AMtOCs) [1].

Other interactions of SNF8

• The N-terminal and C-terminal half of RILP mediate interaction with VPS22 and VPS36, respectively [4].

References