ライフサイエンスコーパス: APC10

1 with Anaphase Promoting Complex Subunit 10 (APC10).

2 perturbing the normal interaction with Doc1/Apc10.

3 -box following repositioning of Cdh1 towards Apc10.

4 degron-recognition module of coactivator and APC10.

5 artite D-box receptor with the APC/C subunit Apc10.

6 ired for its ubiquitination activity is Doc1/Apc10, a protein composed of a Doc1 homology domain that

7 ral cavity of the APC/C assembled from Cdh1, Apc10--a core APC/C subunit previously implicated in sub

8 ubstrate recognition module (Apc2, Apc11 and Apc10 (also known as Doc1)), and TPR-phosphorylation sit

9 Next to APC10 and CDKD, we tested several additional baits in th

10 nally important and conserved region of Doc1/Apc10 and, since invariant residues of Doc1/Apc10 coloca

11 with Anaphase-Promoting Complex subunit 10 (APC10) and Cell Division Cycle 20.1 (CDC20.1), 2 substra

12 rice ANAPHASE PROMOTING COMPLEX SUBUNIT 10 (APC10) and CYCLIN-DEPENDENT KINASE D (CDKD) proteins fro

13 ntains Apc2 (Cullin), Apc11 (RING), and Doc1/Apc10, and another that contains the three TPR subunits

14 l structure of Saccharomyces cerevisiae Doc1/Apc10 at 2.2A resolution.

15 /Apc10 and, since invariant residues of Doc1/Apc10 colocalise with conserved residues of other Doc1 h

16 romote direct association of Cdc20, Cdh1 and Apc10-Doc1 with core APC/C subunits, we propose that thi

17 served protein (a homologue of budding yeast Apc10/Doc1) and is required for ubiquitination and degra

18 tations is due to disruption of the Anapc10 (Apc10/Doc1) gene.

19 of the anaphase-promoting complex component APC10/DOC1.

20 A subpopulation of Apc10 does co-immunoprecipitate with the anaphase-promot

21 Apc10 does not co-sediment with the 20S APC-cyclosome, a

22 f function of one subunit of the APC complex APC10 exhibited a similar phenotype to that of overexpre

23 tor binding with specific disruption of Doc1/Apc10 function in processive ubiquitylation.

24 APC lacking Apc9p or Doc1p/Apc10 have impaired E3 ligase activities.

25 Cdh1 and Apc10, identified from difference maps, create a co-rece

26 c10 interactions, consistent with a role for Apc10 in directly contributing towards D-box recognition

27 R spectroscopy we demonstrate specific D-box-Apc10 interactions, consistent with a role for Apc10 in

28 apc10(+) is essential for viability, encodes a conserved

29 These results imply that Doc1p/Apc10 may play a role to regulate the binding of specifi

30 quitin ligase for B-type cyclins, and in the apc10 mutant the 20S complex is intact, suggesting that

31 The apc10 mutants, previously unidentified, show, in additio

32 ration of Cdc27p into the APC complex, Doc1p/Apc10 plays a specific role in substrate recognition by

33 Residues that are invariant amongst Doc1/Apc10 sequences, including a temperature-sensitive mitot

34 Three loci (apc10, ste9/srw1 and rum1) were identified.

35 adation by linking the activator to the Doc1/Apc10 subunit of core APC/C to stabilize the active holo