The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20

Xuelian Luo, Zhanyun Tang, Jose Rizo-Rey, Hongtao Yu

Research output: Contribution to journalArticle

233 Scopus citations

Abstract

Mad2 participates in spindle checkpoint inhibition of APCCdc20. We show that RNAi-mediated suppression of Mad1 function in mammalian cells causes loss of Mad2 kinetochore localization and impairment of the spindle checkpoint. Mad1 and Cdc20 contain Mad2 binding motifs that share a common consensus. We have identified a class of Mad2 binding peptides with a similar consensus. Binding of one of these ligands, MBP1, triggers an extensive rearrangement of the tertiary structure of Mad2. Mad2 also undergoes a similar striking structural change upon binding to a Mad1 or Cdc20 binding motif peptide. Our data suggest that, upon checkpoint activation, Mad1 recruits Mad2 to unattached kinetochores and may promote binding of Mad2 to Cdc20.

Original languageEnglish (US)
Pages (from-to)59-71
Number of pages13
JournalMolecular cell
Volume9
Issue number1
DOIs
StatePublished - Jan 1 2002

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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