The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20.
Mad2 participates in spindle checkpoint inhibition of APC(Cdc20). 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.
Mesh Terms:
Calcium-Binding Proteins, Cell Cycle Proteins, Hela Cells, Humans, Ligands, Models, Molecular, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Conformation, Proteins, Repressor Proteins
Calcium-Binding Proteins, Cell Cycle Proteins, Hela Cells, Humans, Ligands, Models, Molecular, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Conformation, Proteins, Repressor Proteins
Mol. Cell
Date: Jan. 01, 2002
PubMed ID: 11804586
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