HMMR/RHAMM recruits SACK1D/FAM83D-CK1α complex at the mitotic spindle to control spindle alignment.

ABSTRACT: The SACK1D/FAM83D-CK1α complex assembles at the mitotic spindle to orchestrate proper spindle positioning and error-free progression through mitosis. The full molecular picture of how this complex assembles and disassembles over the cell division cycle remains to be fully defined. Here, we show that hyaluronan-mediated motility receptor (HMMR) is critical for SACK1D-CK1α complex formation at the spindle, co-localizes with the SACK1D-CK1α complex throughout mitosis, and is necessary for correct mitotic spindle alignment. We find that HMMR binds to the C-terminal α-helix of SACK1D, and this helix is also important for the mitotic interaction between SACK1D and CK1α. We demonstrate that HMMR binding stabilizes SACK1D. We map the mitotic hyperphosphorylation sites on SACK1D and show that this

SUBMITTER: Cartwright TN 

PROVIDER: S-EPMC12803952 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature