The beta-isoform of the BRCA2 and CDKN1A(p21)-interacting protein (BCCIP) stabilizes nuclear RPL23/uL14.
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.
['Wyler|Emanuel|E|', 'Wandrey|Franziska|F|', 'Badertscher|Lukas|L|', 'Montellese|Christian|C|', 'Alper|Daniel|D|', 'Kutay|Ulrike|U|']
D021581:Active Transport, Cell Nucleus D024682:BRCA2 Protein D002135:Calcium-Binding Proteins D018797:Cell Cycle Proteins D002467:Cell Nucleus D039642:Eukaryotic Initiation Factors D057809:HEK293 Cells D006801:Humans D009687:Nuclear Proteins D011485:Protein Binding D020033:Protein Isoforms D055550:Protein Stability D012269:Ribosomal Proteins
BCCIP RPL23/uL14 Ribosomal protein Eukaryotic initiation factor 6 (eIF6) Ribosome biogenesis