E2F and cell cycle control: a double-edged sword

Stevens, Craig; La Thangue, Nicholas B

doi:10.1016/s0003-9861(03)00054-7

The Role of Autophagy in Crohn’s Disease (2012)
Journal Article
Henderson, P., & Stevens, C. (2012). The Role of Autophagy in Crohn’s Disease. Cells, 1(3), 492-519. https://doi.org/10.3390/cells1030492

(Macro)-autophagy is a homeostatic process by which eukaryotic cells dispose of protein aggregates and damaged organelles. Autophagy is also used to degrade micro-organisms that invade intracellularly in a process termed xenophagy. Genome-wide associ... Read More about The Role of Autophagy in Crohn’s Disease.

The intermediate filament protein, vimentin, is a regulator of NOD2 activity (2012)
Journal Article
Stevens, C., Henderson, P., Nimmo, E. R., Soares, D. C., Dogan, B., Simpson, K. W., …Satsangi, J. (2013). The intermediate filament protein, vimentin, is a regulator of NOD2 activity. Gut, 62(5), 695-707. https://doi.org/10.1136/gutjnl-2011-301775

Objective Mutations in the nucleotide-binding oligomerisation domain-containing protein 2 (NOD2) gene remain the strongest genetic determinants for Crohn's disease (CD). Having previously identified vimentin as a novel NOD2-interacting protein, the a... Read More about The intermediate filament protein, vimentin, is a regulator of NOD2 activity.

TLE1 modifies the effects of NOD2 in the pathogenesis of Crohn's Disease (2011)
Journal Article
Nimmo, E. R., Stevens, C., Phillips, A. M., Smith, A., Drummond, H. E., Noble, C. L., …Satsangi, J. (2011). TLE1 modifies the effects of NOD2 in the pathogenesis of Crohn's Disease. Gastroenterology, 141(3), 972-981.e2. https://doi.org/10.1053/j.gastro.

Background & Aims The mechanisms by which specific mutations in NOD2/CARD15 increase the risk for Crohn's disease (CD) are unclear. We identified proteins that interact with {NOD2} and investigated them by expression, genetic, and functional analyses... Read More about TLE1 modifies the effects of NOD2 in the pathogenesis of Crohn's Disease.

Tuberous sclerosis-2 (TSC2) regulates the stability of death-associated protein kinase-1 (DAPK) through a lysosome-dependent degradation pathway (2010)
Journal Article
Hupp, T., Lin, Y., Henderson, P., Pettersson, S., Satsangi, J., Hupp, T. R., & Stevens, C. (2010). Tuberous sclerosis-2 (TSC2) regulates the stability of death-associated protein kinase-1 (DAPK) through a lysosome-dependent degradation pathway. FEBS Journ

We previously identified a novel interaction between tuberous sclerosis-2 (TSC2) and death-associated protein kinase-1 (DAPK), the consequence being that DAPK catalyses the inactivating phosphorylation of TSC2 to stimulate mammalian target of rapamyc... Read More about Tuberous sclerosis-2 (TSC2) regulates the stability of death-associated protein kinase-1 (DAPK) through a lysosome-dependent degradation pathway.

Peptide Combinatorial Libraries Identify TSC2 as a Death-associated Protein Kinase (DAPK) Death Domain-binding Protein and Reveal a Stimulatory Role for DAPK in mTORC1 Signaling (2009)
Journal Article
Stevens, C., Lin, Y., Harrison, B., Burch, L., Ridgway, R. A., Sansom, O. J., & Hupp, T. R. (2009). Peptide Combinatorial Libraries Identify TSC2 as a Death-associated Protein Kinase (DAPK) Death Domain-binding Protein and Reveal a Stimulatory Role for DAPK in mTORC1 Signaling. Journal of Biological Chemistry, 284, 334-344. https://doi.org/10.1074/jbc.M805165200

Death-associated protein kinase (DAPK) is a multidomain enzyme that plays a central role in autophagic and apoptotic signaling, although the protein-protein interactions regulating DAPK functions are not well defined. Peptide aptamer libraries were u... Read More about Peptide Combinatorial Libraries Identify TSC2 as a Death-associated Protein Kinase (DAPK) Death Domain-binding Protein and Reveal a Stimulatory Role for DAPK in mTORC1 Signaling.

Death‐associated protein kinase (DAPK) and signal transduction: blebbing in programmed cell death. (2009)
Journal Article
Bovellan, M., Fritzsche, M., Stevens, C., & Charras, G. (2010). Death‐associated protein kinase (DAPK) and signal transduction: blebbing in programmed cell death. FEBS Journal, 277(1), 58-65. https://doi.org/10.1111/j.1742-4658.2009.07412.x

Death-associated protein kinase (DAPK) is a stress-regulated protein kinase that mediates a range of processes, including signal-induced cell death and autophagy. Although the kinase domain of DAPK has a range of substrates that mediate its signallin... Read More about Death‐associated protein kinase (DAPK) and signal transduction: blebbing in programmed cell death..

Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death: DAPK and signal transduction (2009)
Journal Article
Lin, Y., Hupp, T. R., & Stevens, C. (2010). Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death: DAPK and signal transduction. FEBS Journal, 277(1), 48-57. https://doi.org/10.1111/j.1742-4658.2009.07411.x

Death-associated protein kinase (DAPK) is a stress-regulated protein kinase that mediates a range of processes, including signal-induced cell death and autophagy. Although the kinase domain of DAPK has a range of substrates that mediate its signalli... Read More about Death-associated protein kinase (DAPK) and signal transduction: additional roles beyond cell death: DAPK and signal transduction.

Autophagy: from basic science to clinical application (2009)
Journal Article
Van Limbergen, J., Stevens, C., Nimmo, E. R., Wilson, D. C. & Satsangi, J. (2009). Autophagy: from basic science to clinical application. Mucosal immunology. 2. (4). 315-330. doi:10.1038/mi.2009.20. ISSN 1933-0219.

Autophagy is a cellular pathway involved in protein and organelle degradation, which is likely to represent an innate adaptation to starvation. In times of nutrient deficiency, the cell can self-digest and recycle some nonessential components through... Read More about Autophagy: from basic science to clinical application.

The alternative splice variant of DAPK-1, s-DAPK-1, induces proteasome-independent DAPK-1 destabilization. (2009)
Journal Article
Lin, Y., Stevens, C., Harrison, B., Pathuri, S., Amin, E., & Hupp, T. R. (2009). The alternative splice variant of DAPK-1, s-DAPK-1, induces proteasome-independent DAPK-1 destabilization. Molecular and Cellular Biochemistry, 328(1-2), (101-107). doi:10.10

Death-associated protein kinase 1 (DAPK-1) is a Ca2+/CaM-regulated kinase involved in multiple cellular signalling pathways that trigger cell survival, apoptosis, and autophagy. An alternatively spliced product expressed from the dapk1 locus, named s... Read More about The alternative splice variant of DAPK-1, s-DAPK-1, induces proteasome-independent DAPK-1 destabilization..

ATP stimulates MDM2-mediated inhibition of the DNA-binding function of E2F1: ATP stimulated inhibition of E2F1 by MDM2 (2008)
Journal Article
Stevens, C., Pettersson, S., Wawrzynow, B., Wallace, M., Ball, K., Zylicz, A., & Hupp, T. R. (2008). ATP stimulates MDM2-mediated inhibition of the DNA-binding function of E2F1: ATP stimulated inhibition of E2F1 by MDM2. FEBS Journal, 275(19), 4875-4886. https://doi.org/10.1111/j.1742-4658.2008.06627.x

Murine double minute 2 (MDM2) protein exhibits many diverse biochemical functions on the tumour suppressor protein p53, including transcriptional suppression and E3 ubiquitin ligase activity. However, more recent data have shown that MDM2 can exhibit... Read More about ATP stimulates MDM2-mediated inhibition of the DNA-binding function of E2F1: ATP stimulated inhibition of E2F1 by MDM2.

An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing: Functional transcript expressed by DAPK-1 locus (2008)
Journal Article
Lin, Y., Stevens, C., Hrstka, R., Harrison, B., Fourtouna, A., Pathuri, S., …Hupp, T. (2008). An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing: Functional transcri

Death-associated protein kinase 1 (DAPK-1) is a multidomain protein kinase with diverse roles in autophagic, apoptotic and survival pathways. Bioinformatic screens were used to identify a small internal mRNA from the DAPK-1 locus (named s-DAPK-1). Th... Read More about An alternative transcript from the death-associated protein kinase 1 locus encoding a small protein selectively mediates membrane blebbing: Functional transcript expressed by DAPK-1 locus.

Novel insights into DAPK autophagic signalling using peptide aptamer combinatorial protein-interaction screens (2008)
Journal Article
Stevens, C. & Hupp, T. R. (2008). Novel insights into DAPK autophagic signalling using peptide aptamer combinatorial protein-interaction screens. Autophagy. 4. (4). 531-533. doi:10.4161/auto.5940. ISSN 1554-8627.

DAPK represents a relatively unique enzyme in the protein kinase superfamily whose major biological functions are linked to both autophagy and signal-mediated apoptosis. However, genetic studies have not yet uncovered how DAPK integrates into the cor... Read More about Novel insights into DAPK autophagic signalling using peptide aptamer combinatorial protein-interaction screens.

DAPK-1 Bbnding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing (2008)
Journal Article
Harrison, B., Kraus, M., Burch, L., Stevens, C., Craig, A., Gordon-Weeks, P., & Hupp, T. R. (2008). DAPK-1 Bbnding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing. Journal of Biological Chemistry, 283(15), 9999-10014. https:/

DAPK-1 (death-activated protein kinase) has wide ranging functions in cell growth control; however, DAPK-1 interacting proteins that mediate these effects are not well defined. Protein-protein interactions are driven in part by linear interaction mot... Read More about DAPK-1 Bbnding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing.

Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. (2007)
Journal Article
Lin, Y., Stevens, C., & Hupp, T. (2007). Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. Journal of Biological Chemistry, 282(23), 16792-16802. https://doi.org/10.107

DAPK-1 is a stress-activated tumor suppressor protein that plays a role in both proapoptotic or antiapoptotic signal transduction pathways. To define mechanisms of DAPK-1 protein regulation, we have determined that DAPK-1 protein has a long half-life... Read More about Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis..

A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis (2007)
Journal Article
Stevens, C., Lin, Y., Sanchez, M., Amin, E., Copson, E., White, H., …Hupp, T. (2007). A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis. Journal of Biological Chemistry, 282(18), 13791-13803. https://doi.org/10.1074/jb

p53 is activated genetically by a set of kinases that are components of the calcium calmodulin kinase superfamily, including CHK2, AMP kinase, and DAPK-1. In dissecting the mechanism of DAPK-1 control, a novel mutation (N1347S) was identified in the... Read More about A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis.

The emerging role of E2F-1 in the DNA damage response and checkpoint control. (2004)
Journal Article
Stevens, C., & La Thangue, N. B. (2004). The emerging role of E2F-1 in the DNA damage response and checkpoint control. DNA Repair, 3(8-9), 1071-1079. https://doi.org/10.1016/j.dnarep.2004.03.034

Genotoxic stress triggers a myriad of cellular responses including cell cycle arrest, stimulation of {DNA} repair and apoptosis. A central role for the E2F-1 transcription factor in the {DNA} damage response pathway is gaining support. E2F-1 is phosp... Read More about The emerging role of E2F-1 in the DNA damage response and checkpoint control..

A New Role for E2F-1 in Checkpoint Control (2003)
Journal Article
Stevens, C., & Thangue, N. B. L. (2003). A New Role for E2F-1 in Checkpoint Control. Cell Cycle, 2(5), 434-436. https://doi.org/10.4161/cc.2.5.462

In response to DNA damage, E2F-1 is induced and phosphorylated. Phosphorylated E2F-1 can reside in discrete nuclear structures and induce apoptosis, suggesting a unique role for E2F-1 in DNA repair and checkpoint functions.

Chk2 activates E2F-1 in response to DNA damage (2003)
Journal Article
Stevens, C., Smith, L., & La Thangue, N. B. (2003). Chk2 activates E2F-1 in response to DNA damage. Nature Cell Biology, 5(5), 401-409. https://doi.org/10.1038/ncb974

The E2F-1 transcription factor is regulated during cell cycle progression and induced by cellular stress, such as DNA damage. We report that checkpoint kinase 2 (Chk2) regulates E2F-1 activity in response to the DNA-damaging agent etoposide. A Chk2 c... Read More about Chk2 activates E2F-1 in response to DNA damage.

E2F and cell cycle control: a double-edged sword (2003)
Journal Article
Stevens, C., & La Thangue, N. B. (2003). E2F and cell cycle control: a double-edged sword. Archives of Biochemistry and Biophysics, 412(2), 157-169. https://doi.org/10.1016/s0003-9861%2803%2900054-7

The E2F family of transcription factors plays a central role in regulating cellular proliferation by controlling the expression of both the genes required for cell cycle progression, particularly DNA synthesis, and the genes involved with apoptosis.... Read More about E2F and cell cycle control: a double-edged sword.

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