The abstract is read at the publisher; the summary is JClub's.
FCS-calibrated molecular counting in living cells shows CENP-C is present at roughly double the copy number of other constitutive centromere-associated network components, including CENP-T.
- Why it matters: Structural work has clarified kinetochore architecture in vitro, but the molecular organization and protein abundance at the kinetochore in living cells remains unclear.
- What they did: The authors used fluorescence correlation spectroscopy with an absolute counting framework to quantify kinetochore protein copy numbers, then tested KMN recruitment when CENP-T or CENP-C lacks the Mis12C-binding domain.
- The result: Loss of either CENP-T or CENP-C Mis12C-binding domain leaves a redundant pathway that sustains Ndc80C recruitment, enabling theory-grounded molecular abundance maps of the kinetochore in cells.
The findingWhy it mattersWhat they didThe result
AI summary of the abstract · may contain errors · not medical advice · read the paper.