Dynein light chain DLC-1 promotes localization and function of the PUF protein FBF-2 in germline progenitor cells

Xiaobo Wang, Jenessa R. Olson, Dominique Rasoloson, Mary Ellenbecker, Jessica Bailey, Ekaterina Voronina

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

PUF family translational repressors are conserved developmental regulators, but the molecular function provided by the regions flanking the PUF RNA-binding domain is unknown. In C. elegans, the PUF proteins FBF-1 and FBF-2 support germline progenitor maintenance by repressing production of meiotic proteins and use distinct mechanisms to repress their target mRNAs. We identify dynein light chain DLC-1 as an important regulator of FBF-2 function. DLC-1 directly binds to FBF-2 outside of the RNA-binding domain and promotes FBF-2 localization and function. By contrast, DLC-1 does not interact with FBF-1 and does not contribute to FBF-1 activity. Surprisingly, we find that the contribution of DLC-1 to FBF-2 activity is independent of the dynein motor. Our findings suggest that PUF protein localization and activity are mediated by sequences flanking the RNA-binding domain that bind specific molecular partners. Furthermore, these results identify a new role for DLC-1 in posttranscriptional regulation of gene expression.

Original languageEnglish
Pages (from-to)4643-4653
Number of pages11
JournalDevelopment (Cambridge)
Volume143
Issue number24
DOIs
StatePublished - Dec 15 2016

Keywords

  • Germline
  • LC8 family proteins
  • Post-transcriptional regulation
  • RNA-binding protein
  • Stem cells

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