A novel Jun N‐terminal kinase (JNK)‐binding protein that enhances the activation of JNK by MEK kinase 1 and TGF‐β‐activated kinase 1

Koyano, Satoru; Ito, Michihiko; Takamatsu, Nobuhiko; Shiba, Tadayoshi; Yamamoto, Ken; Yoshioka, Katsuji

doi:10.1016/s0014-5793(99)01084-4

Cited by 22 publications

(32 citation statements)

References 29 publications

(30 reference statements)

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“…JNKBP1 was initially identified in mice as a protein interacting with JNK and playing a scaffold role in the JNK-dependent pathway (16). This function is independent on N-terminal WD-40 domain but involves a region in the C-terminal part (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Expression of JNKBP1 in Human Cell Lines and in the Intestine-Little is known about the tissue distribution of JNKBP1 in humans, whereas it has been shown to be ubiquitously expressed in mouse tissues and principally in the brain (16). To assess the expression of human JNKBP1 in various kinds of cells, we determined the levels of JNKBP1 mRNA in different human cell lines by qRT-PCR.…”

Section: Identification Of Jnkbp1 As a Nod2-interacting Protein-tomentioning

confidence: 99%

“…Mouse JNKBP1, also named mitogen-activated protein kinase-binding protein 1 (MAPKBP1), was initially identified in a yeast two-hybrid system used to search for proteins interacting with JNK3 (16). JNKBP1 contains 12 WD-40 repeats in the N-terminal part and a JNK-binding region located in the C-terminal region (16).…”

mentioning

confidence: 99%

“…JNKBP1 contains 12 WD-40 repeats in the N-terminal part and a JNK-binding region located in the C-terminal region (16). JNKBP1 appears to be ubiquitously expressed in mouse tissues and to play a scaffold function in JNK signaling.…”

mentioning

confidence: 99%

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The c-Jun N-terminal Kinase (JNK)-binding Protein (JNKBP1) Acts as a Negative Regulator of NOD2 Protein Signaling by Inhibiting Its Oligomerization Process

Lecat

Valentin

Somja

et al. 2012

Journal of Biological Chemistry

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Background: NOD2 belongs to the NLR family. JNKBP1, a scaffold protein, is characterized by an N-terminal WD-40 domain. Results: JNKBP1 is co-expressed with NOD2 in epithelial and immune cells of intestine mucosa. Binding of JNKB1 to NOD2 attenuates NOD2 signaling by inhibiting its oligomerization. Conclusion: JNKBP1 is a new NOD2 modulator. Significance: JNKBP1, by down-regulating NOD2 signaling, could contribute to maintaining intestinal immune homeostasis.

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Section: Discussionmentioning

confidence: 99%

Section: Identification Of Jnkbp1 As a Nod2-interacting Protein-tomentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The c-Jun N-terminal Kinase (JNK)-binding Protein (JNKBP1) Acts as a Negative Regulator of NOD2 Protein Signaling by Inhibiting Its Oligomerization Process

Lecat

Valentin

Somja

et al. 2012

Journal of Biological Chemistry

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“…The pcDNA3 His-S-JNK2 expression vector was described previously (39). The ORF of Xenopus caspase-8 was amplified from Xenopus liver cDNA by PCR using two primers, 5Ј-AGTGACCTGTTAAGTTCTA-CAGT-3Ј and 5Ј-TTACATGGCATTAGGAGGTGG-3Ј.…”

Section: Materials-thementioning

confidence: 99%

Xenopus Death Receptor-M1 and -M2, New Members of the Tumor Necrosis Factor Receptor Superfamily, Trigger Apoptotic Signaling by Differential Mechanisms

Tamura

Noyama

Ishizawa

et al. 2004

Journal of Biological Chemistry

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Signaling through the tumor necrosis factor receptor (TNFR) superfamily can lead to apoptosis or promote cell survival, proliferation, and differentiation. A subset of this family, including TNFR1 and Fas, signals cell death via an intracellular death domain and therefore is termed the death receptor (DR) family. In this study, we identified new members of the DR family, designated xDR-M1 and xDR-M2, in Xenopus laevis. The two proteins, which show high homology (71.7% identity), have characteristics of the DR family, that is, three cysteinerich domains, a transmembrane domain, and a death domain. To elucidate how members of xDR-M subfamily regulate cell death and survival, we examined the intracellular signaling mediated by these receptors in 293T and A6 cells. Overexpression of xDR-M2 induced apoptosis and activated caspase-8, c-Jun N-terminal kinase, and nuclear factor-B, although its death domain to a greater extent than did that of xDR-M1 in 293T cells. A caspase-8 inhibitor potently blocked this apoptosis induced by xDR-M2. In contrast, xDR-M1 showed a greater ability to induce apoptosis through its death domain than did xDR-M2 in A6 cells. Interestingly, a general serine protease inhibitor, but not the caspase-8 inhibitor, blocked the xDR-M1-induced apoptosis. These results imply that activation of caspase-8 or serine protease(s) may be required for the xDR-

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The Role of WD40-Repeat Protein 62 (MCPH2) in Brain Growth: Diverse Molecular and Cellular Mechanisms Required for Cortical Development

Shohayeb

Lim

et al. 2017

Mol Neurobiol

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Genetic disruptions of spindle/centrosome-associated WD40-repeat protein 62 (WDR62) are causative for autosomal recessive primary microcephaly (MCPH) and a broader range of cortical malformations. Since the identification of WDR62 as encoded by the MCPH2 locus in 2010, recent studies that have deleted/depleted WDR62 in various animal models of cortical development have highlighted conserved functions in brain growth. Here, we provide a timely review of our current understanding of WDR62 contributions in the self-renewal, expansion and fate specification of neural stem and progenitor cells that are critical for neocortical development. Recent studies have revealed multiple functions for WDR62 in the regulation of spindle organization, mitotic progression and the duplication and biased inheritance of centrosomes during asymmetric divisions. We also discuss recently elaborated WDR62 interaction partners that include Aurora and c-Jun N-terminal kinases as part of complex signalling mechanisms that may define its neural functions. These studies provide new insights into the molecular and cellular processes that are required for brain formation and implicated in the genesis of primary microcephaly.

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A novel Jun N‐terminal kinase (JNK)‐binding protein that enhances the activation of JNK by MEK kinase 1 and TGF‐β‐activated kinase 1

Cited by 22 publications

References 29 publications

The c-Jun N-terminal Kinase (JNK)-binding Protein (JNKBP1) Acts as a Negative Regulator of NOD2 Protein Signaling by Inhibiting Its Oligomerization Process

The c-Jun N-terminal Kinase (JNK)-binding Protein (JNKBP1) Acts as a Negative Regulator of NOD2 Protein Signaling by Inhibiting Its Oligomerization Process

Xenopus Death Receptor-M1 and -M2, New Members of the Tumor Necrosis Factor Receptor Superfamily, Trigger Apoptotic Signaling by Differential Mechanisms

The Role of WD40-Repeat Protein 62 (MCPH2) in Brain Growth: Diverse Molecular and Cellular Mechanisms Required for Cortical Development

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