ライフサイエンスコーパス: alpha-COP

1 alpha-COP binds to SMN, linking the COPI vesicular trans

2 lpha-COP, Nucleolin acts an adaptor to allow alpha-COP to interact with a population of mRNA.

3 We have previously shown that SMN and alpha-COP interact and co-migrate in axons, and that ove

4 e p1 CPY; these defects can be suppressed by alpha-COP overproduction.

5 ypically Golgi associated, in neuronal cells alpha-COP localizes to lamellipodia and growth cones and

6 nsmembrane proteins are captured by coatomer alpha-COP and beta'-COP subunits and packaged into COPI-

7 ogenous Nucleolin co-precipitates endogenous alpha-COP and epsilon-COP but not beta-COP which may ref

8 ate binding of KKxx motifs by the homologous alpha-COP domain.

9 Remarkably, heterologous expression of human alpha-COP restored normal neurite length and morphology

10 ecognition motif appears to reside solely in alpha-COP, antibody-induced supershift strongly indicate

11 nce, found within alpha-COP itself, mediates alpha-COP homo-oligomerization.

12 The last approximately 170 amino acids of alpha-COP are also non-essential for cell viability, but

13 Through in vivo analysis of alpha-COP truncation mutants, we characterize distinct f

14 mplex between the C-terminal domain (CTD) of alpha-COP and full-length epsilon-COP, two components of

15 Depletion of alpha-COP resulted in mislocalization of SMN and actin a

16 nerated a point mutant in the WD40 domain of alpha-COP which eliminates its ability to co-precipitate

17 ne motif of Nucleolin and the WD40 domain of alpha-COP, Nucleolin acts an adaptor to allow alpha-COP

18 Reduced levels of alpha-COP restricted development of neuronal processes i

19 34 degrees C, through stabilizing levels of alpha-COP.

20 We identified single amino acid mutants of alpha-COP that selectively abrogate SMN binding, retain

21 migrate in axons, and that overexpression of alpha-COP reduced phenotypic severity in cell culture an

22 mmunoblot analysis confirmed the presence of alpha-COP in the Mono-Q fraction as well as that of a se

23 We present crystal structures of alpha-COP and beta'-COP bound to a series of naturally o

24 characterize distinct functional domains on alpha-COP.

25 tdIns(3,4,5)P3-displaceable labeling of only alpha-COP.

26 at a function of epsilon-COP is to stabilize alpha-COP and the coatomer complex.

27 The COPI coatomer subunit alpha-COP has been shown to co-precipitate mRNA in multi

28 dentify a conserved site on the COPI subunit alpha-COP that binds to flexible, acidic sequences conta

29 Binding experiments show that alpha-COP and beta'-COP have generally the same specific

30 Together, our findings suggest that alpha-COP homo-oligomerization plays a key role in COPI

31 The alpha-COP CTD adopts a U-shaped architecture that comple

32 The alpha-COP protein co-immunoprecipitates with SMN, small

33 The alpha-COP(CTD) x epsilon-COP complex forms heterodimers

34 The alpha-COP(CTD) x epsilon-COP heterodimer forms a rod-sha

35 a missense mutation in the gene encoding the alpha-COP subunit of the COPI complex (COPA).

36 D-3 and D-5 phosphates are critical for the alpha-COP-PtdIns(3,4,5)P3 interaction, suggesting an imp

37 raps around a protruding beta-hairpin of the alpha-COP CTD, thus interlocking the two proteins.

38 splaceable photocovalent modification of the alpha-COP subunit was observed with a p-benzoyldihydroci

39 s suggested that the 140-kDa protein was the alpha-COP subunit of coatomer protein COPI, usually asso

40 The ability of Nucleolin to bind to alpha-COP requires the presence of the C-terminal KKxKxx

41 lta cells shifted to 37 degrees C, wild-type alpha-COP (Ret1p) levels diminish rapidly and cells accu

42 vel yeast alpha-COP mutant, ret1-3, in which alpha-COP is degraded after cells are shifted to a restr

43 elated with the strength of interaction with alpha-COP.

44 -specific synthetic-lethal interactions with alpha-COP mutations: sec28 Delta ret1-3 double mutants a

45 One such sequence, found within alpha-COP itself, mediates alpha-COP homo-oligomerizatio

46 We isolated a novel yeast alpha-COP mutant, ret1-3, in which alpha-COP is degraded