Binding of Par-4 to the actin cytoskeleton is essential for Par-4/Dlk-mediated apoptosis

Vetterkind, Susanne; Illenberger, Susanne; Kubíček, Jan; Boosen, Meike; Appel, Sarah; Naim, Hassan Y.; Scheidtmann, Karl Heinz; Preuß, Ute

doi:10.1016/j.yexcr.2005.01.012

Cited by 34 publications

(71 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…9 In differentiating ES cells, however, we found that PAR-4 was co-distributed with F-actin to a high extent without resulting in apoptosis. Using an antibody against DLK we could not detect its expression in differentiating ES cells (data not shown).…”

Section: Role Of Exon 3 In Par-4-induced Apoptosismentioning

confidence: 63%

“…5,6 There has been, however, an ongoing controversy with respect to the subcellular site at which PAR-4 induces apoptosis. 8,9 To determine the subcellular localization of PAR-4 in embryoid body (EB)-derived cells (EBCs), we performed immunocytochemistry on different stages of EBC differentiation ( Figure 1A and 1B). Consistent with our previous studies, we found that PAR-4 was localized in both the cytosol and the nucleus.…”

Section: Differentiation-stage Specific Expression Of Two Par-4 Isofomentioning

confidence: 99%

“…8 In another study using mouse 3T3 fibroblasts, PAR-4 was found to be predominantly co-localized with F-actin. 9 The authors suggested that an N-terminal domain of 266 amino acids was critical for direct binding of PAR-4 to F-actin and the induction of apoptosis by a complex formed between PAR-4 and DAP-like kinase (DLK).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A novel isoform of prostate apoptosis response 4 (PAR-4) that co-distributes with F-actin and prevents apoptosis in neural stem cells

et al. 2006

View full text Add to dashboard Cite

The elevated expression of prostate apoptosis response-4 (PAR-4) induces apoptosis in differentiating mouse embryonic stem (ES) cells. In embryoid body (EB) cells and the E15.5 stage of embryonic mouse brain, PAR-4 is expressed as two isoforms (38 and 33 kDa). Using mouse EB-derived RNA as a template we have cloned and characterized a novel isoform of PAR-4 (PAR-4/p33) that lacks exon 3 and shows a bona fide splice junction of exons 2 and 4. The molecular mass for PAR-4/p33 is estimated to be 33 kDa, corresponding to the short form found in the EB cells and E15.5 mouse brain. The fluorescent fusion protein of PAR-4/p33 is mainly found in the cytosol and is co-distributed with F-actin filaments, while that of the 38 kDa full length PAR-4/p38 is predominantly translocated to the nucleus. In contrast to the full length PAR-4 (PAR-4/p38), ectopic expression of PAR-4/p33 does not result in the activation of caspase 3 and the induction of apoptosis. PAR-4/p33 forms a complex with PAR-4/p38, which inhibits its nuclear translocation and the induction of apoptosis. PAR-4/p33 is suggested to be a dominant negative isoform of PAR-4/p38 and may regulate PAR-4-dependent apoptosis.

show abstract

Section: Role Of Exon 3 In Par-4-induced Apoptosismentioning

confidence: 63%

Section: Differentiation-stage Specific Expression Of Two Par-4 Isofomentioning

confidence: 99%

See 1 more Smart Citation

A novel isoform of prostate apoptosis response 4 (PAR-4) that co-distributes with F-actin and prevents apoptosis in neural stem cells

et al. 2006

View full text Add to dashboard Cite

show abstract

“…In addition to its pro-apoptotic functions, PAR-4 has been shown to regulate the activity of choline acetyl transferase, to inhibit choline uptake, and to regulate synaptic plasticity [133][134][135] . In this regard, it may be of interest that PAR-4 has been found to be temporarily associated with the actin cytoskeleton [136] . Our group has described a short form of PAR-4 that acts as dominant negative regulator of apoptosis by forming actin-associated heterodimers with the pro-apoptotic long form of PAR-4 [6] .…”

Section: Lipid Rafts and Slips: A Platform For Cell Signaling Pathwaysmentioning

confidence: 99%

Smart Drugs for Smarter Stem Cells: Making SENSe (Sphingolipid-Enhanced Neural Stem Cells) of Ceramide

Bieberich

2008

Neurosignals

View full text Add to dashboard Cite

Ceramide and its derivative sphingosine-1-phosphate (S1P) are important signaling sphingolipids for neural stem cell apoptosis and differentiation. Most recently, our group has shown that novel ceramide analogs can be used to eliminate teratoma (stem cell tumor)-forming cells from a neural stem cell graft. In new studies, we found that S1P promotes survival of specific neural precursor cells that undergo differentiation to cells expressing oligodendroglial markers. Our studies suggest that a combination of novel ceramide and S1P analogs eliminates tumor-forming stem cells and at the same time, triggers oligodendroglial differentiation. This review discusses recent studies on the function of ceramide and S1P for the regulation of apoptosis, differentiation, and polarity in stem cells. We will also discuss results from ongoing studies in our laboratory on the use of sphingolipids in stem cell therapy.

show abstract

“…ZIPK has been shown to phosphorylate STAT3 on Ser-727, thus enhancing the transcriptional activity of STAT3 (7). Vetterkind et al (8) have demonstrated that prostate apoptosis response-4 (Par-4), which is characterized mainly as a proapoptotic protein, targets ZIPK to the cytoskeleton in nonmuscle cells, leading to apoptosis. By contrast, in smooth muscle cells, Par-4 supports contractility by targeting ZIPK to the cytoskeleton (9).…”

Section: Introductionmentioning

confidence: 99%

Zipper-interacting protein kinase interacts with human cell division cycle 14A phosphatase

et al. 2014

Molecular Medicine Reports

View full text Add to dashboard Cite

Abstract. Zipper-interacting protein kinase (ZIPK) is a novel serine/threonine protein kinase and a member of a large family of protein kinases, known as the death-associated protein kinases. However, the function of ZIPK has yet to be fully elucidated, as few physiological substrates have currently been identified. In the present study, a yeast two-hybrid screen was used and the human cell division cycle 14A (HsCdc14A) phosphatase was identified as a novel ZIPK binding protein.To the best of our knowledge, this is the first study to report the interaction between these proteins. The interaction between ZIPK and HsCdc14A was confirmed by in vitro experiments. In addition, ZIPK-mediated phosphorylation was shown to activate the phosphatase activity of HsCdc14A. These findings indicated that ZIPK may also be involved in the regulation of the cell cycle in human cells, by interacting with HsCdc14A.

show abstract

Binding of Par-4 to the actin cytoskeleton is essential for Par-4/Dlk-mediated apoptosis

Cited by 34 publications

References 58 publications

A novel isoform of prostate apoptosis response 4 (PAR-4) that co-distributes with F-actin and prevents apoptosis in neural stem cells

A novel isoform of prostate apoptosis response 4 (PAR-4) that co-distributes with F-actin and prevents apoptosis in neural stem cells

Smart Drugs for Smarter Stem Cells: Making SENSe (Sphingolipid-Enhanced Neural Stem Cells) of Ceramide

Zipper-interacting protein kinase interacts with human cell division cycle 14A phosphatase

Contact Info

Product

Resources

About