ライフサイエンスコーパス: CENP-F

1 CENP-F is a nonmotor microtubule-binding protein that pa

2 CENP-F is important for the formation of proper kinetoch

3 CENP-F, hBUBR1, and CENP-E assembled onto kinetochores i

4 CENP-F-driven mitochondrial transport is linked to growi

5 CP-4 are both required for localization of a CENP-F-like protein, HCP-1, indicating an ordered assemb

6 t throughout the mitotic delay some aligned, CENP-F depleted kinetochores continuously recruit Mad1.

7 f dynein at G2/M that facilitates BICD2- and CENP-F-mediated anchoring of dynein to nuclear pore comp

8 er kinetochore components, such as BubR1 and CENP-F, on centromeres.

9 f these, the centromeric proteins CENP-E and CENP-F are preferentially expressed during mitosis and a

10 RhoB and the centromere proteins CENP-E and CENP-F are relevant targets of farnesylation inhibition;

11 rom the COOH-terminal CAAX box of CENP-E and CENP-F are substrates for farnesyl transferase but not g

12 t preventing the farnesylation of CENP-E and CENP-F by treatment with the farnesyl transferase inhibi

13 of the outer kinetochore proteins CENP-E and CENP-F, which are involved in chromosome congression and

14 n than kinetochore recruitment of CENP-E and CENP-F.

15 arnesylated centromeric proteins, CENP-E and CENP-F.

16 CENP-E (centromere protein E) and CENP-F (centromere protein F), also known as mitosin, ar

17 n without affecting RZZ complex, CENP-E, and CENP-F KT localization.

18 lization of RanGAP1, Mad1, Mad2, CENP-E, and CENP-F, as well as loss of cold-stable kinetochore-MT in

19 We characterized CENP-F(+/+) and CENP-F(-/-) mouse embryonic fibroblasts (MEFs) and found

20 rotubule tips can transport mitochondria and CENP-F-coated artificial cargoes over micrometer-long di

21 CENP-E's C-terminus and CENP-F's N-terminus bind microtubules with similar affin

22 ch as anti-p53, anti-p62, anti-Koc, and anti-CENP-F, auto-antibodies to p90 represent a new marker fo

23 ted the dynamic association of LANA and Bub1/CENP-F and the colocalization between Bub1, LANA, and th

24 We characterized CENP-F(+/+) and CENP-F(-/-) mouse embryonic fibroblasts

25 at included the kinetochore proteins CENP-E, CENP-F, and hBUBR1, a BUB1-related kinase that was found

26 Centromere protein F (CENP-F) (or mitosin) accumulates to become an abundant n

27 Centromere protein F (CENP-F) has been shown to include two MT-binding domains

28 D2 (BICD2) and Nup133- centromere protein F (CENP-F) networks.

29 ociation of LANA with centromeric protein F (CENP-F) prompted us to further study whether LANA target

30 crotubule (MT)-binding centromere protein F (CENP-F) was previously shown to play a role exclusively

31 lated association with centromere protein F (CENP-F), allowing ATR to engage replication protein A (R

32 novel and critical localization and role for CENP-F at the centrosome, the major MT organizing center

33 ivation and silencing and a crucial role for CENP-F in efficient assembly of a stable microtubule-kin

34 A polypeptide from CENP-F's C terminus also bound MTs, and either protein f

35 ata, we hypothesize that chicken CMF1, human CENP-F, mitosin, and mouse LEK1 are members of an emergi

36 splice variant of the closely related human CENP-F, serves a similar function to LEK1 in humans.

37 murine cDNA, LEK1, that is related to human CENP-F and mitosin and more distantly to chicken CMF1.

38 ed structural and checkpoint proteins HZW10, CENP-F and Mad2p.

39 d 3-5 pN but could exceed 10 pN, identifying CENP-F as a highly effective coupler to shortening MTs.

40 zation is readily observed from the Golgi in CENP-F(-/-) cells.

41 ber of outer kinetochore proteins, including CENP-F [1, 2] and the widely conserved microtubule-assoc

42 Many studies have linked CENP-F to MT-based activities as disruption of this prot

43 Here we show that the absence of nuclear CENP-F does not affect cell cycle progression in S and G

44 The "RanBP2-BicD2" and "Nup133-CENP-F" pathways act sequentially, with Nup133 or CENP-F

45 mechanisms involving RanBP2-BicD2 and Nup133-CENP-F.

46 (-/-) cells, we demonstrate that ablation of CENP-F protein function eliminates MT repolymerization a

47 Still, the basis of CENP-F regulation of the MT network remains elusive.

48 research demonstrating the strong binding of CENP-F to the MT network, support the conclusion that CE

49 olymerization block shows that disruption of CENP-F function impacts MT nucleation and anchoring rath

50 how that the N-terminal MT-binding domain of CENP-F prefers curled oligomers of tubulin relative to M

51 the amino- and carboxyl-terminal domains of CENP-F as well as the carboxyl-terminal (non-kinesin) do

52 ent is triggered by a Cdk1-induced export of CENP-F from the nucleus.

53 als a major new localization and function of CENP-F at the centrosome that is likely to impact a broa

54 The centrosome-specific function of CENP-F in the regulation of MT growth is confirmed by ex

55 raction and reveal the novel localization of CENP-F at the centrosome.

56 In contrast, the majority of CENP-F depleted cells exhibit a strong mitotic delay wit

57 Many cell models of CENP-F depletion show a lag in the cell cycle and aneupl

58 k at the centrosome, as a binding partner of CENP-F.

59 Importantly, in this first report of CENP-F(-/-) cells, we demonstrate that ablation of CENP-

60 In a subset of CENP-F depleted cells, kinetochore assembly fails comple

61 hanism distinct from that of either BICD2 or CENP-F.

62 F" pathways act sequentially, with Nup133 or CENP-F RNAi arresting nuclei close to the ventricular su

63 on between LANA and the kinetochore proteins CENP-F and Bub1 is important for KSHV genome tethering a

64 relationship between HCP-1/2, two redundant CENP-F-like proteins, and CLASP(CLS-2) in Caenorhabditis

65 the MT network, support the conclusion that CENP-F is a powerful regulator of MT dynamics during int

66 We discovered that CENP-F(-/-) MEFs have severely diminished MT dynamics, w

67 r novel genetic deletion model, we show that CENP-F also regulates a broader range of cellular functi

68 Here we show that CENP-F tracks growing microtubule ends in living cells.

69 e and previous observations, we suggest that CENP-F might act as a transporter of mitochondria and ot

70 show that the conserved kinesin CeMCAK, the CENP-F-related proteins HCP-1 and HCP-2, and the core ki

71 mino and carboxy termini of LANA can bind to CENP-F.

72 owth is confirmed by expression of truncated CENP-F containing only the Hook2-binding domain.

73 Using CENP-F as a marker for progress through G2, we also show

74 the well-characterized Ndc80 complex, while CENP-F's C-terminus shows much lower affinity.

75 We detected G2 cells with CENP-F, a nuclear protein maximally expressed in G2.

76 Here we show that LANA colocalized with CENP-F as speckles, some of which are paired at centrome

77 le 1), which is known to form a complex with CENP-F.

78 es, whereas no dramatic effect was seen with CENP-F knockdown.