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 language | English (US) |
|---|---|
| Pages (from-to) | 665-675 |
| Number of pages | 11 |
| Journal | Journal of Cell Biology |
| Volume | 174 |
| Issue number | 5 |
| DOIs | |
| State | Published - Aug 28 2006 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
Cite this
The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope. / Jaspersen, Sue L.; Martin, Adriana E.; Glazko, Galina; Giddings, Thomas H.; Morgan, Garry; Mushegian, Arcady; Winey, Mark.
In: Journal of Cell Biology, Vol. 174, No. 5, 28.08.2006, p. 665-675.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope
AU - Jaspersen, Sue L.
AU - Martin, Adriana E.
AU - Glazko, Galina
AU - Giddings, Thomas H.
AU - Morgan, Garry
AU - Mushegian, Arcady
AU - Winey, Mark
PY - 2006/8/28
Y1 - 2006/8/28
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33748119341&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33748119341&partnerID=8YFLogxK
U2 - 10.1083/jcb.200601062
DO - 10.1083/jcb.200601062
M3 - Article
C2 - 16923827
AN - SCOPUS:33748119341
VL - 174
SP - 665
EP - 675
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 5
ER -