High impact information on POF1B

• Because POF1B shares high homology with the tail portion of the human myosin, we assessed the ability of both wild-type and mutant POF1B proteins to bind nonmuscle actin filaments in vitro [1].
• Disruption of POF1B binding to nonmuscle actin filaments is associated with premature ovarian failure [1].
• Our study suggests that a homozygous point mutation in POF1B influences the pathogenesis of POF by altering POF1B binding to nonmuscle actin filaments [1].
• We found that the capacity of the mutant protein to bind nonmuscle actin filaments was diminished fourfold compared with the wild type, suggesting a function of POF1B in germ-cell division [1].
• We performed a mutation analysis of POF1B and of another gene previously identified, DACH2, localized approximately 700 kb distal in Xq21, in a cohort of >200 Italian POF patients [2].

Biological context of POF1B

• METHODS AND RESULTS: By fine mapping of the X chromosome breakpoint of an X;autosome balanced translocation, we identified a new interrupted gene, POF1B [2].
• CONCLUSIONS: Our findings could not demonstrate any involvement of POF1B, but suggest that rare mutations in the DACH2 gene may have a role in the POF phenotype [2].
• By sequencing one candidate gene within that region, POF1B, we identified a point mutation localized in exon 10 [1].

Other interactions of POF1B

• Mutation analysis of two candidate genes for premature ovarian failure, DACH2 and POF1B [2].
• Two genes, FRAXA and POF1B, have been formally demonstrated to be responsible for POF [3].

References