The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope

Sue L. Jaspersen, Adriana E. Martin, Galina Glazko, Thomas H. Giddings, Garry Morgan, Arcady Mushegian, Mark Winey

Research output: Contribution to journalArticle

99 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)665-675
Number of pages11
JournalJournal of Cell Biology
Volume174
Issue number5
DOIs
StatePublished - Aug 28 2006
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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