The beta-isoform of the BRCA2 and CDKN1A(p21)-interacting protein (BCCIP) stabilizes nuclear RPL23/uL14

FEBS Lett. 2014 Oct 16;588(20):3685-91. doi: 10.1016/j.febslet.2014.08.013. Epub 2014 Aug 19.


BRCA2 and CDKN1A(p21,CIP1)-interacting protein (BCCIP) is an evolutionary conserved protein implicated in maintenance of genome stability and cell cycle progression. Two isoforms of BCCIP with distinct C-terminal domains exist in humans. We show that mammalian BCCIPβ, but not BCCIPα, forms a ternary complex with the ribosomal protein RPL23/uL14 and the pre-60S trans-acting factor eIF6. Complex formation is dependent on an intact C-terminal domain of BCCIPβ. Depletion of BCCIPβ reduces the pool of free RPL23, and decreases eIF6 levels in nucleoli. Overexpression of BCCIPβ leads to nucleoplasmic accumulation of extra-ribosomal RPL23 and stabilizes overexpressed RPL23, suggesting that BCCIPβ functions as nuclear chaperone for RPL23.

Keywords: BCCIP; Eukaryotic initiation factor 6 (eIF6); RPL23/uL14; Ribosomal protein; Ribosome biogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • BRCA2 Protein / metabolism*
  • Calcium-Binding Proteins / metabolism*
  • Cell Cycle Proteins / metabolism*
  • Cell Nucleus / metabolism*
  • Eukaryotic Initiation Factors / metabolism
  • HEK293 Cells
  • Humans
  • Nuclear Proteins / metabolism*
  • Protein Binding
  • Protein Isoforms / metabolism
  • Protein Stability
  • Ribosomal Proteins / metabolism*


  • BCCIP protein, human
  • BRCA2 Protein
  • BRCA2 protein, human
  • Calcium-Binding Proteins
  • Cell Cycle Proteins
  • EIF6 protein, human
  • Eukaryotic Initiation Factors
  • Nuclear Proteins
  • Protein Isoforms
  • Ribosomal Proteins
  • ribosomal protein L17