| Autor: |
Heinrich, Stephanie, Sewart, Katharina, Windecker, Hanna, Langegger, Maria, Schmidt, Nadine, Hustedt, Nicole, Hauf, Silke |
| Zdroj: |
EMBO Reports; Mar2014, Vol. 15 Issue 3, p291-298, 10p |
| Abstrakt: |
The spindle assembly checkpoint inhibits anaphase until all chromosomes have become attached to the mitotic spindle. A complex between the checkpoint proteins Mad1 and Mad2 provides a platform for Mad2: Mad2 dimerization at unattached kinetochores, which enables Mad2 to delay anaphase. Here, we show that mutations in Bub1 and within the Mad1 C-terminal domain impair the kinetochore localization of Mad1:Mad2 and abrogate checkpoint activity. Artificial kinetochore recruitment of Mad1 in these mutants co-recruits Mad2; however, the checkpoint remains non-functional. We identify specific mutations within the C-terminal head of Mad1 that impair checkpoint activity without affecting the kinetochore localization of Bub1, Mad1 or Mad2. Hence, Mad1 potentially in conjunction with Bub1 has a crucial role in checkpoint signalling in addition to presenting Mad2. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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