ライフサイエンスコーパス: RACK

1 RACK-1 binding to IFN-alphaRbetaL did not require the fi

2 RACK-1 is also required for proper chromosome separation

3 RACK-1 itself did not become tyrosine phosphorylated upo

4 RACK-1 localizes to the centrosomes, kinetochores, the m

5 RACK-1 was shown to be constitutively associated with IF

6 is elegans Receptor of Activated C Kinase 1 (RACK-1) is required for cytokinesis, germline membrane o

7 , mitogen-activated protein kinase kinase 5, RACK 1, apolipoprotein C-III, and the gene encoding the

8 s increases the interaction between NR2B and RACK-1, which is also dependent on tPA, further suggesti

9 ng leukocyte protein of 76 kDa), p62dok, and RACK-1 (receptor for activated protein kinase C-1).

10 eraction between the psiepsilonRACK site and RACK-binding site within epsilonPKC is critical and rate

11 platelets, PKC-theta-selective antagonistic (RACK; receptor for activated C kinase) peptide significa

12 Our findings indicate that INAD functions as RACK (receptor for activated PKC), allowing eye-PKC to p

13 The interaction between RACK-1 and IFN-alphaRbetaL, but not the human IFN recept

14 translocation of PKCepsilon and PKCbetaI by RACK interference peptides attenuated EGF-mediated preve

15 ein receptor for activated protein kinase C (RACK)-1 has been linked to a variety of signaling system

16 PKC-interacting proteins collectively called RACKs (Receptors for Activated C-Kinases).

17 s for activated C kinase collectively called RACKs.

18 -selective proteins were called collectively RACKs (receptors for activated C-kinase).

19 Furthermore, administration of psi(epsilon)RACK before ischemia followed by deltaV1-1 during reperf

20 In contrast, pretreatment with psi(epsilon)RACK but not deltaV1-1, followed by a 10-minute washout

21 continuous systemic delivery of psi(epsilon)RACK confers sustained cardioprotection against ischemia

22 adverse effects after sustained psi(epsilon)RACK delivery.

23 inistration of deltaV1-1 but not psi(epsilon)RACK during reperfusion improved cardiac function and de

24 ction, continuous treatment with psi(epsilon)RACK induced a sustained preconditioned state during the

25 The epsilonPKC activator psi(epsilon)RACK induced cardioprotection both in vivo and ex vivo,

26 Thus, psi(epsilon)RACK may be useful for patients with ischemic heart dise

27 In addition, the psi(epsilon)RACK peptide should be a useful pharmacological agent fo

28 psi(epsilon)RACK treatment reduced infarct size (34+/-2% versus 14+/

29 solated mouse hearts and whether psi(epsilon)RACK treatment reduces infarct size or lethal arrhythmia

30 schemia-reperfusion in vivo, and psi(epsilon)RACK was administered by intracoronary injection during

31 After psi(epsilon)RACK was systemically administered in mice either acutel

32 % versus 14+/-1%, control versus psi(epsilon)RACK) and resulted in fewer cases of ventricular fibrill

33 V1-1) and epsilon-PKC activator (psi(epsilon)RACK) peptides for ischemia/reperfusion damage in isolat

34 87.5% versus 50%, control versus psi(epsilon)RACK).

35 epsilon-protein kinase C (PKC), psi(epsilon)RACK, conferred cardioprotection against ischemia-reperf

36 Whereas psi(epsilon)RACK-induced cardioprotection lasted 1 hour after a sing

37 addition, pretreatment of platelets with eta-RACK antagonistic peptides, a specific inhibitor of nPKC

38 ain of IFN-alphaRbetaL, the minimum site for RACK-1 binding was mapped to aa 300-346.

39 ills the criteria previously established for RACKs.

40 However, RACK-1 should play a broader role in type I IFN signalin

41 ddition to anchoring activated PKC isozymes, RACKs anchor other signaling enzymes.

42 r interaction with a sequence resembling its RACK, termed psiepsilonRACK.

43 silonPKC first translocates and binds to its RACK and subsequently the epsilonPKC/epsilonRACK complex

44 r hidden when active epsilonPKC binds to its RACK.

45 ins such as receptor for activated C kinase (RACK) 1 are involved in the targeting of signaling prote

46 s, such as receptors for activated C kinase (RACKs), play an important role in regulating the localiz

47 ns such as receptors for activated C kinase (RACKs).

48 proteins (receptors for activated C kinases (RACKs)) and demonstrates a direct connection between the

49 Last, RACK-1 may facilitate the sequestration of recycling end

50 In overlay assays with native RACK-1 that had been immobilized on nitrocellulose, UV-t

51 phaRbetaL did not require the first 91 aa of RACK-1, which includes two WD domains, WD1 and WD2.

52 rescence and intracellular redistribution of RACK-1.

53 The role of RACKs in PKC-mediated signaling was determined using iso

54 slocation by inhibiting formation of the PKC.RACK-1 complex.

55 As expected for a PKCepsilon RACK binding peptide, confocal microscopy showed that ep

56 y shown that at least part of the PKCepsilon RACK-binding site on PKCepsilon lies within the unique V

57 aRbetaL and a previously identified protein, RACK-1 (receptor for activated C kinase).

58 he binding of each isozyme to its respective RACK.

59 on V1 region to clone a PKCepsilon-selective RACK, which was identified as the COPI coatomer protein,

60 RACK2, the epsilonPKC-specific RACK, is a coated-vesicle protein and thus is involved i

61 ing of the activated isozyme to its specific RACK, epsilonRACK.

62 ediated by their binding to isozyme-specific RACKs (receptors for activated C-kinase).

63 1 and a point mutant that does not bind Src (RACK Y246F) with green fluorescent protein and expressed

64 In the IFN system, RACK-1 functions as an adaptor recruiting the transcript

65 o isozyme-specific anchoring proteins termed RACKs, accompany protein kinase C (PKC) activation.

66 In this study, we demonstrate that RACK-1 serves as a scaffold protein for a multiprotein c

67 Finally, we provide evidence that RACK-1 may also serve as a scaffold protein in other cyt

68 We found that RACK-1 directly binds to DNC-2, the C. elegans p50/dynam

69 ment of synthetic peptides modeled after the RACK-1-binding site in the C2 region of PKC beta induced

70 ypothesized that in inactive epsilonPKC, the RACK-binding site is engaged in an intramolecular intera

71 type I IFN signaling because mutation of the RACK-1 binding site in the IFN-alpha receptor 2/beta sub

72 Therefore, RACKs are not only adaptors for PKC, but also serve as a

73 in human platelets pretreated with PKC-theta RACK peptide, which may contribute to the lower levels o

74 ion (Ki = 11.5 +/- 5 microM) with respect to RACK-1 (receptor for activated C kinase-1), an adaptor p

75 , UV-treated control PKC alpha bound well to RACK-1, whereas UV/DECA-inactivated PKC alpha had reduce

76 e at least some of the proteins that bind to RACKs, including PKC itself, regulate cell growth, modul

77 be a result of inhibition of its binding to RACKs due to Nef binding, could contribute to the variou

78 Our findings suggest a mechanism by which RACK-1 directs the dynactin-dependent redistribution of

79 l growth, modulating their interactions with RACKs may help elucidate signaling pathways leading to c