Fleeting Amyloid-like Forms of Rim4 Ensure Meiotic Fidelity

Alice Flynn Ford; James Shorter

doi:10.1016/j.cell.2015.09.049

Fleeting Amyloid-like Forms of Rim4 Ensure Meiotic Fidelity

Cell. 2015 Oct 8;163(2):275-6. doi: 10.1016/j.cell.2015.09.049.

Authors

Alice Flynn Ford¹, James Shorter²

Affiliations

¹ Department of Biochemistry and Biophysics, Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA; Neuroscience Graduate Group, Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA.
² Department of Biochemistry and Biophysics, Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA; Neuroscience Graduate Group, Perelman School of Medicine at The University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: jshorter@mail.med.upenn.edu.

Abstract

Berchowitz et al. establish that transient amyloid-like forms of Rim4, a yeast RNA-binding protein with a predicted prion domain, translationally repress cyclin CLB3 in meiosis I, thereby ensuring homologous chromosome segregation. These findings suggest that prion domains might enable formation of tightly regulated amyloid-like effectors in diverse functional settings.

Publication types

Comment

MeSH terms

Animals
Gametogenesis*
Male
Protein Aggregates*
RNA-Binding Proteins / metabolism*
Saccharomyces cerevisiae Proteins / metabolism*

Substances

Protein Aggregates
RNA-Binding Proteins
Saccharomyces cerevisiae Proteins

Grants and funding

R01 GM099836/GM/NIGMS NIH HHS/United States