Septin1, a new interaction partner for human serine/threonine kinase aurora-B

Qi, Ming; Yu, Wenbo; Liu, Shen; Jia, Huijue; Tang, Luosheng; Shen, Mingjuan; Yan, Xiaomei; Saiyin, Hexige; Lang, Qingyu; Wan, Bo; Zhao, Shengming; Liu, Yu

doi:10.1016/j.bbrc.2005.06.212

Cited by 46 publications

(51 citation statements)

References 34 publications

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“…17). Whatever the details, the (118), desmin (119), and septin (120), and binds to survivin (121) and vimentin (122). APC/C, anaphasepromoting complex/cyclosome; CENPA, centromere protein A; Eg5, kinesin-like protein; H3, histone 3; Nlp, ninein-like protein; NudC, nuclear distribution gene C. data show that mitotic arrest is not maintained for any extended period.…”

Section: Duration Of Mitotic Arrestmentioning

confidence: 98%

Inhibitors Targeting Mitosis: Tales of How Great Drugs against a Promising Target Were Brought Down by a Flawed Rationale

Komlódi-Pásztor

Sackett

Fojo

2012

Clinical Cancer Research

196

175

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Although they have been advocated with an understandable enthusiasm, mitosis-specific agents such as inhibitors of mitotic kinases and kinesin spindle protein have not been successful clinically. These drugs were developed as agents that would build on the success of microtubule-targeting agents while avoiding the neurotoxicity that encumbers drugs such as taxanes and vinca alkaloids. The rationale for using mitosisspecific agents was based on the thesis that the clinical efficacy of microtubule-targeting agents could be ascribed to the induction of mitotic arrest. However, the latter concept, which has long been accepted as dogma, is likely important only in cell culture and rapidly growing preclinical models, and irrelevant in patient tumors, where interference with intracellular trafficking on microtubules is likely the principal mechanism of action. Here we review the preclinical and clinical data for a diverse group of inhibitors that target mitosis and identify the reasons why these highly specific, myelosuppressive compounds have failed to deliver on their promise.

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Section: Duration Of Mitotic Arrestmentioning

confidence: 98%

Inhibitors Targeting Mitosis: Tales of How Great Drugs against a Promising Target Were Brought Down by a Flawed Rationale

Komlódi-Pásztor

Sackett

Fojo

2012

Clinical Cancer Research

196

175

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“…SEPT2 and SEPT3) contain multiple phosphorylation sites and are phosphorylated by Ser/Thr kinases such as protein kinase C (PKC) and cGMP-dependent protein kinase I (PKG-I) in post-mitotic neurons (She et al, 2004;Xue et al, 2004a;Xue et al, 2004b;Xue et al, 2000) and by Aurora-B kinase in mitotic cells (e.g. SEPT1) (Qi et al, 2005). Thus, sumoylation and phosphorylation of septins might act as conformational switches that alter their polymerization and thereby functions.…”

Section: Assembly and Regulation Of Septin Polymersmentioning

confidence: 99%

Here come the septins: novel polymers that coordinate intracellular functions and organization

Spiliotis

Nelson

2006

Journal of Cell Science

149

130

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Septins are conserved GTP-binding proteins that associate with cellular membranes and the actin and microtubule cytoskeletons. They polymerize to form filamentous structures that act as diffusion barriers between different membrane domains and as molecular scaffolds for membrane- and cytoskeleton-binding proteins. In yeast, septins are central to the spatio-temporal coordination of membrane polarity and cell division, but the roles of their mammalian counterparts have remained poorly understood. However, recent findings have shed light on the dynamics and regulation of mammalian septin assembly and our understanding of septin functions in cytoskeleton and membrane organization. The mammalian septins appear to form a novel network of hetero-polymers that are multi-functional, inter-changeable and respond dynamically to signals that coordinate events at the interface between cytoskeleton and membrane biology. Hence, studies of these molecules might provide new insights not only into how cells coordinate their functions, but also into the pathogenesis of cancer and other diseases in which septins are abnormally expressed.

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“…However, previous studies have identified several mammalian septins as substrates of several kinases. For instance, SEPT1 has been shown to be phosphorylated in vitro by aurora-B kinase [41] . SEPT2 is a substrate of casein kinase 2, and its phosphorylation on Ser-218 is crucial for the proliferation of hepatoma carcinoma cells [44] .…”

Section: Discussionmentioning

confidence: 99%

“…In previous studies, several septins have been shown to be phosphorylated in vitro and/or in vivo, including SEPT1, SEPT2, SEPT3 and SEPT5 [40][41][42][43][44] . After describing the interaction between two proteins, we wanted to know whether MK5 possesses catalytic activity towards SEPT8.…”

Section: Mk5 Phosphorylates Sept8 In Vitromentioning

confidence: 95%

Septin 8 is an interaction partner and in vitro substrate of MK5

Shiryaev

Kostenko²,

Dumitriu³

et al. 2012

WJBC

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AIM:To identify novel substrates for the mitogen-activated protein kinase-activated protein kinase 5 (MK5). METHODS:Yeast two-hybrid screening with MK5 as bait was used to identify novel possible interaction partners. The binding of putative partner was further examined by glutathione S-transferase (GST) pull-down, co-immunoprecipitation and fluorescence resonance energy transfer (FRET) analysis. In vitro kinase and peptide array assays were used to map MK5 phosphoacceptor sites on the new partner. Confocal microscopy was performed to study the subcellular localization of MK5 and its partners. RESULTS:Septin 8 was identified as a novel interaction partner for MK5 by yeast two-hybrid screening. This interaction was confirmed by GST pull-down, coimmunoprecipitation and FRET analysis. Septin 5, which can form a complex with septin 8, did not interact with MK5. Serine residues 242 and 271 on septin 8 were identified as in vitro MK5 phosphorylation sites. MK5and septin 8 co-localized in the perinuclear area and in cell protrusions. Moreover, both proteins co-localized with vesicle marker synaptophysin. CONCLUSION:Septin 8 is a bona fide interaction partner and in vitro substrate for MK5. This interaction may be implicated in vesicle trafficking.

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Septin1, a new interaction partner for human serine/threonine kinase aurora-B

Cited by 46 publications

References 34 publications

Inhibitors Targeting Mitosis: Tales of How Great Drugs against a Promising Target Were Brought Down by a Flawed Rationale

Inhibitors Targeting Mitosis: Tales of How Great Drugs against a Promising Target Were Brought Down by a Flawed Rationale

Here come the septins: novel polymers that coordinate intracellular functions and organization

Septin 8 is an interaction partner and in vitro substrate of MK5

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