지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2018.3
- 수록면
- 436 - 443 (8page)
- DOI
- 10.14348/molcells.2018.2266
이용수
초록· 키워드
오류제보하기
The actin cytoskeleton plays a key role in the entry of mitosis as well as in cytokinesis. In a previous study, we showed that actin disruption delays mitotic entry at G2/M by sustained activation of extracellular signal-related kinase 1/2 (ERK1/2) in primary cells but not in transformed cancer cell lines. Here, we examined the mechanism of cell cycle delay at G2/M by actin dysfunction in IMR-90 normal human fibroblasts. We ob-served that de-polymerization of actin with cytochalasin D (CD) constitutively activated ribosomal S6 kinase (RSK) and induced inhibitory phosphorylation of Cdc2 (Tyr 15) in IMR-90 cells. In the presence of an actin defect in IMR-90 cells, activating phosphorylation of Wee1 kinase (Ser 642) and inhibitory phosphorylation of Cdc25C (Ser 216) was also maintained. However, when kinase-dead RSK (DN-RSK) was overexpressed, we observed sustained activation of ERK1/2, but no delay in the G2/M transition, demonstrating that RSK functions downstream of ERK in cell cycle delay by actin dysfunction. In DN-RSK overexpressing IMR-90 cells treated with CD, phosphorylation of Cdc25C (Ser 216) was blocked and phosphorylation of Cdc2 (Tyr 15) was decreased, but the phosphorylation of Wee1 (Ser 642) was maintained, demonstrating that RSK directly controls phosphorylation of Cdc25C (Ser 216), but not the activity of Wee1. These results strongly suggest that actin dysfunction in primary cells activates ERK1/2 to inhibit Cdc2, delaying the cell cycle at G2/M by activating downstream RSK, which phosphorylates and blocks Cdc25C, and by directly activating Wee1.
목차
등록된 정보가 없습니다.
참고문헌 (29)
참고문헌 신청
Alphine, A.E. / 2001 / Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1 / J. Cell Biol. 153:273~282
Asano, E. / 2011 / Role of palladin phosphorylation by extracellular signal-regulated kinase in cell migration / PloS One 6:e29338
Bulavin, D.V. / 2003 / Dual phosphorylation controls Cdc25 phosphatases and mitotic entry / Nat. Cell Biol. 5:545~551
Carreno, S. / 2008 / Moesin and its activating kinase Slik are required for cortical stability and microtubule organization in mitotic cells / J. Cell Biol. 180:739~746
Chun, J. / 2005 / Phosphorylation of Cdc25C by p90RSK contributes to the G2 cell cycle arrest in Xenopus Cycling Egg extracts / Cell Cycle 4:148~154
Asano, E. / 2011 / Role of palladin phosphorylation by extracellular signal-regulated kinase in cell migration / PloS One 6:e29338
Bulavin, D.V. / 2003 / Dual phosphorylation controls Cdc25 phosphatases and mitotic entry / Nat. Cell Biol. 5:545~551
Carreno, S. / 2008 / Moesin and its activating kinase Slik are required for cortical stability and microtubule organization in mitotic cells / J. Cell Biol. 180:739~746
Chun, J. / 2005 / Phosphorylation of Cdc25C by p90RSK contributes to the G2 cell cycle arrest in Xenopus Cycling Egg extracts / Cell Cycle 4:148~154
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