ライフサイエンスコーパス: APC10

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1 degron-recognition module of coactivator and APC10.

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

3 -box following repositioning of Cdh1 towards Apc10.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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