Nek2A specifies the centrosomal localization of Erk2

Lou, Yang; Xie, Wei; Zhang, Dongfang; Yao, Jianhui; Luo, Zhaofeng; Wang, Yuzhen; Shi, Yunyu; Yao, Xuebiao

doi:10.1016/j.bbrc.2004.06.171

Cited by 19 publications

(15 citation statements)

References 28 publications

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“…We therefore suggest this is because in normal conditions appropriate expression of TEIF may be necessary to ensure the homeostasis of centrosomes, whereas its overexpression is a dominant event in spontaneous tumorigenesis. Similar mechanics of operation have in fact been identified in other centrosomal factors such as TACC, cep135, Nek2 or Aurora A kinase (Ohta et al, 2002;Stenoien et al, 2003;Dou et al, 2004;Lou et al, 2004;Peset and Vernos, 2008).…”

Section: Discussionsupporting

confidence: 63%

“…For instance, the classic centrosome protein TACC2 and some regulators such as Erk2, p53 and BRCA1 distribute into centrosomes after phosphorylation (Dou et al, 2004;Lou et al, 2004;McPherson et al, 2006). However, in contrast to the putative N-terminal STYKc (Ser/Thr/Tyr) kinase-like domain, the C terminus of TEIF has no conserved functional domains shared with proteins in either the centrosome or other compartments.…”

Section: Discussionmentioning

confidence: 99%

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Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

et al. 2009

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Section: Discussionsupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

et al. 2009

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“…GTPbound Ras activates Raf1 kinase and assembles Raf, the dual specificity kinases MEK1/2 and the p42/p44 MAP kinases extracellular signal-regulated kinase (ERK)1/2 into a membrane-bound phosphorylation cascade in which Raf1 phosphorylates MEK1/2, which in turn activate ERK, which is then released from the complex and translocates to the nucleus and other cellular sites (Besson et al, 2001;Lou et al, 2004;Torii et al, 2004b). Active nuclear ERK promotes the transcription of D-type cyclins and the cyclin-dependent kinase inhibitor p21Cip1, constituting a necessary step in G 1 exit and S-phase entry.…”

Section: Introductionmentioning

confidence: 99%

Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G₂Phase and Promotes the G₂/M Cell Cycle Transition

Feinstein

Linstedt

2007

MBoC

101

162

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Two controversies have emerged regarding the signaling pathways that regulate Golgi disassembly at the G2/M cell cycle transition. The first controversy concerns the role of mitogen-activated protein kinase activator mitogen-activated protein kinase kinase (MEK)1, and the second controversy concerns the participation of Golgi structure in a novel cell cycle “checkpoint.” A potential simultaneous resolution is suggested by the hypothesis that MEK1 triggers Golgi unlinking in late G2 to control G2/M kinetics. Here, we show that inhibition of MEK1 by RNA interference or by using the MEK1/2-specific inhibitor U0126 delayed the passage of synchronized HeLa cells into M phase. The MEK1 requirement for normal mitotic entry was abrogated if Golgi proteins were dispersed before M phase by treatment of cells with brefeldin A or if GRASP65, which links Golgi stacks into a ribbon network, was depleted. Imaging revealed that unlinking of the Golgi apparatus begins before M phase, is independent of cyclin-dependent kinase 1 activation, and requires MEK signaling. Furthermore, expression of the GRASP family member GRASP55 after alanine substitution of its MEK1-dependent mitotic phosphorylation sites inhibited both late G2 Golgi unlinking and the G2/M transition. Thus, MEK1 plays an in vivo role in Golgi reorganization, which regulates cell cycle progression.

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“…In this regard, activated (phosphorylated) MEK1/2 and ERK1/2 are reported by immunofluorescence (IMF) to be present during mitosis in centrosomes/spindle poles (Shapiro et al, 1998;Liu et al, 2004;Lou et al, 2004) and kinetochores (Shapiro et al, 1998;Zecevic et al, 1998) where it is proposed to play a role in the SAC (Shapiro et al, 1998;Willard and Crouch, 2001;Horne and Guadagno, 2003). However, there is little data to support a functional role at these locations and that which does is indirect and open to different interpretations.…”

Section: Introductionmentioning

confidence: 99%

Extracellular Signal-regulated Kinase 1/2 Activity Is Not Required in Mammalian Cells during Late G₂for Timely Entry into or Exit from Mitosis

Shinohara

Mikhailov

Aguirre‐Ghiso

et al. 2006

MBoC

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Extracellular signal-regulated kinase (ERK)1/2 activity is reported to be required in mammalian cells for timely entry into and exit from mitosis (i.e., the G 2 -mitosis [G 2 /M] and metaphase-anaphase [M/A] transitions). However, it is unclearwhether this involvement reflects a direct requirement for ERK1/2 activity during these transitions or for activating gene transcription programs at earlier stages of the cell cycle. To examine these possibilities, we followed live cells in which ERK1/2 activity was inhibited through late G 2 and mitosis. We find that acute inhibition of ERK1/2 during late G 2 and through mitosis does not affect the timing of the G 2 /M or M/A transitions in normal or transformed human cells, nor does it impede spindle assembly, inactivate the p38 stress-activated checkpoint during late G 2 or the spindle assembly checkpoint during mitosis. Using CENP-F as a marker for progress through G 2 , we also show that sustained inhibition of ERK1/2 transiently delays the cell cycle in early/mid-G 2 via a p53-dependent mechanism. Together, our data reveal that ERK1/2 activity is required in early G 2 for a timely entry into mitosis but that it does not directly regulate cell cycle progression from late G 2 through mitosis in normal or transformed mammalian cells. INTRODUCTIONThe extracellular signal-regulated (ERK)1/2 pathway consists of Raf1, mitogen-activated protein kinase kinase (MEK)1/2, and ERK1/2 kinases, which upon pathway activation are sequentially and specifically phosphorylated . Once activated, ERK1/2 phosphorylates numerous cytoplasmic and nuclear substrates that lead to diverse cellular responses, including proliferation and differentiation, via both transcription-dependent and independent mechanisms (Pearson et al., 2001;Yoon and Seger, 2006). Basically, ERK1/2 activity is essential for cell growth; it mediates the G 1 /S transition by facilitating nucleotide and protein syntheses as well as the transcription of cell cycle regulators, including cyclins D and E (Widmann et al., 1999;Roovers and Assoian, 2000). Not unexpectedly, constitutive activation of ERK1/2 via mutations in Raf or its upstream Ras G protein leads to uncontrolled cell growth, whereas the inability to activate ERK1/2 is lethal in utero (Wojnowski et al., 1998;Giroux et al., 1999) and inhibits the growth of cultured cells (Pages et al., 1993).In addition to its essential role in promoting the G 1 /S transition, enhanced ERK1/2 activity is also required in mammalian cells for a timely G 2 -mitosis (G 2 /M) transition. Long-term (hours to days) suppression of ERK1/2 by using pharmacological inhibitors of MEK1/2, dominant-negative MEK1, or RNA interference (RNAi) produces a delay in "G 2 /M" (Wright et al., 1999;Hayne et al., 2000;Roberts et al., 2002;Liu et al., 2004;Knauf et al., 2006). Gene expression profiling of nontransformed mammary epithelial cells also reveals that constitutive activation of ERK1/2 via MEK1 leads to increased levels of mRNAs that encode mitotic proteins such as Cyclin B, CDK1, CENP-E, Bub1, Mad...

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Nek2A specifies the centrosomal localization of Erk2

Cited by 19 publications

References 28 publications

Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G₂Phase and Promotes the G₂/M Cell Cycle Transition

Extracellular Signal-regulated Kinase 1/2 Activity Is Not Required in Mammalian Cells during Late G₂for Timely Entry into or Exit from Mitosis

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Nek2A specifies the centrosomal localization of Erk2

Cited by 19 publications

References 28 publications

Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

Localization of TEIF in the centrosome and its functional association with centrosome amplification in DNA damage, telomere dysfunction and human cancers

Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G2Phase and Promotes the G2/M Cell Cycle Transition

Extracellular Signal-regulated Kinase 1/2 Activity Is Not Required in Mammalian Cells during Late G2for Timely Entry into or Exit from Mitosis

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Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G₂Phase and Promotes the G₂/M Cell Cycle Transition

Extracellular Signal-regulated Kinase 1/2 Activity Is Not Required in Mammalian Cells during Late G₂for Timely Entry into or Exit from Mitosis