ライフサイエンスコーパス: epsilon-COP

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1 epsilon-COP (Sec28p) overproduction suppresses the defec

2 epsilon-COP is thus non-essential for yeast cell growth,

3 cluding Clathrin, Sec13-Sec31, and alphabeta'epsilon-COP.

4 in adaptors, and the cargo-binding alphabeta'epsilon-COP B-subcomplex.

5 rieval signals bound the alpha-, beta'-, and epsilon-COP subunits of coatomer, whereas other p24 doma

6 in (GAP) Glo3p, but not Gcs1p, and beta- and epsilon-COP interact with ARF-GTP.

7 subunits, with only beta, beta', delta, and epsilon-COP showing competitive displacement by excess I

8 the domain structure of the alpha-, beta'-, epsilon-COP and beta-, gamma-, delta-, zeta-COP coatomer

9 henotypes arose in mutants deficient in both epsilon-COP and either Cog1 or Cog2.

10 roximately 10 min later by a COPI component (epsilon-COP) and a trans-Golgi network (TGN) marker (GRI

11 the time required for the loss of detectable epsilon-COP, suggesting that the endocytic defects were

12 sential for cell viability, but required for epsilon-COP incorporation into coatomer and maintainance

13 Thus, a mutation in epsilon-COP that causes instability at 39.5 degrees C is

14 Surprisingly, cells lacking epsilon-COP (sec28 Delta) grow well up to 34 degrees C a

15 al domain (CTD) of alpha-COP and full-length epsilon-COP, two components of the B-subcomplex, at a 2.

16 ion into coatomer and maintainance of normal epsilon-COP levels.

17 ltered by small interfering RNA depletion of epsilon-COP in wild-type cells under conditions in which

18 rchitecture that complements the TPR fold of epsilon-COP.

19 Our results suggest that a function of epsilon-COP is to stabilize alpha-COP and the coatomer c

20 re analysis of the structure and function of epsilon-COP, the assembly of COPs into coatomers, and th

21 f the synthesis, structure, and stability of epsilon-COP.

22 lon-COP in ldlF cells was about half that of epsilon-COP in wild-type Chinese hamster ovary cells and

23 f beta-COP is not linked directly to that of epsilon-COP.

24 cells depleted of the temperature-sensitive epsilon-COP subunit.

25 erature-sensitive defect in the COPI subunit epsilon-COP.

26 We show that epsilon-COP depletion for 12 h caused a primary block to

27 Taken together, the results suggest that epsilon-COP acts early in the endocytic pathway, most li

28 The epsilon-COP TPRs form a circular bracelet that wraps aro

29 SEC28 encodes the epsilon-COP subunit of COPI (coat protein complex I) coa

30 ion in ldlF cells of a point mutation in the epsilon-COP gene, Glu251 to Lys251, which prevents the c

31 at they directly or indirectly reflected the epsilon-COP defect.

32 antibodies to ADP-ribosylating factor and to epsilon-COP.

33 nts for the virtual absence of detectable ts-epsilon-COP protein in ldlF cells after incubation at 39

34 (34 degrees C), the steady state level of ts-epsilon-COP in ldlF cells was about half that of epsilon

35 ovary cells and the isoelectric point of ts-epsilon-COP was 0.14 pH units higher than that of the wi

36 The stability but not the biosynthesis of ts-epsilon-COP was temperature-sensitive (t1/2 > 6 h at 34

37 also corrected by transfection of wild-type epsilon-COP cDNA demonstrating that they directly or ind

38 tion with an expression vector for wild-type epsilon-COP, a subunit of coatomers.

39 dimer forms a rod-shaped structure, in which epsilon-COP adopts a tetratricopeptide repeat (TPR) fold

40 The alpha-COP(CTD) x epsilon-COP complex forms heterodimers in solution, and

41 The alpha-COP(CTD) x epsilon-COP heterodimer forms a rod-shaped structure, in

42 e isolated the previously unidentified yeast epsilon-COP gene.

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