ライフサイエンスコーパス: epsilon-COP

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 lin co-precipitates endogenous alpha-COP and epsilon-COP but not beta-COP which may reflect an intera

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

35 (34 degrees C), the steady state level of ts-epsilon-COP in ldlF cells was about half that of epsilon

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

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

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

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

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

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

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

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