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The Sad1-UNC-84 homology domain in Mps3 ... body with the nuclear envelope
The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope.
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The spindle pole body (SPB) is the sole site of microtubule nucleation in Saccharomyces cerevisiae; yet, details of its assembly are poorly understood. Integral membrane proteins including Mps2 anchor the soluble core SPB in the nuclear envelope. Adjacent to the core SPB is a membrane-associated SPB substructure known as the half-bridge, where SPB duplication and microtubule nucleation during G1 occurs. We found that the half-bridge component Mps3 is the budding yeast member of the SUN protein family (Sad1-UNC-84 homology) and provide evidence that it interacts with the Mps2 C terminus to tether the half-bridge to the core SPB. Mutants in the Mps3 SUN domain or Mps2 C terminus have SPB duplication and karyogamy defects that are consistent with the aberrant half-bridge structures we observe cytologically. The interaction between the Mps3 SUN domain and Mps2 C terminus is the first biochemical link known to connect the half-bridge with the core SPB. Association with Mps3 also defines a novel function for Mps2 during SPB duplication.
Jaspersen SL, Martin AE, Glazko G, Giddings TH, Morgan G, Mushegian A, Winey M
The Journal of cell biology
2006-08-28 00:00
174
5
665-75
Amino Acid Sequence,Cell Cycle,Cell Cycle Proteins,Centrosome,Chromosome Segregation,Membrane Proteins,Mitotic Spindle Apparatus,Molecular Sequence Data,Mutation,Nuclear Envelope,Nuclear Proteins,Protein Binding,Protein Structure, Tertiary,Protein-Serine-Threonine Kinases,Saccharomyces cerevisiae,Saccharomyces cerevisiae Proteins,Sequence Alignment,Sequence Homology, Amino Acid,Cell Cycle Proteins,MPS2 protein, S cerevisiae,Membrane Proteins,Mps3 protein, S cerevisiae,Nuclear Proteins,Saccharomyces cerevisiae Proteins,RAD53 protein, S cerevisiae,Protein-Serine-Threonine Kinases
Stowers Institute for Medical Research, Kansas City, MO 64110, USA sljstowers-instituteorg
J. Cell Biol.
NIGMS GM51312
0021-9525
10.1083/jcb.200601062
jcb.200601062
1281
True
16923827
