Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

Jin Woo Kim; Myung Jin Kim; Kwang Je Kim; Hee Jae Yun; Ji Soo Chae; Sang Gil Hwang; Tong Shin Chang; Hee Sae Park; Kang Woo Lee; Pyung Lim Han; Ssang Goo Cho; Tae Wan Kim; Eui Ju Choi

doi:10.1073/pnas.0501600102

Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

Jin Woo Kim, Myung Jin Kim, Kwang Je Kim, Hee Jae Yun, Ji Soo Chae, Sang Gil Hwang, Tong Shin Chang, Hee Sae Park, Kang Woo Lee, Pyung Lim Han, Ssang Goo Cho, Tae Wan Kim, Eui Ju Choi

Divison of Brain & Cognitive Sciences

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

Abstract

The transmembrane protein Notch is cleaved by γ-secretase to yield an active form. Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.

Original language	English
Pages (from-to)	14308-14313
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	102
Issue number	40
DOIs	https://doi.org/10.1073/pnas.0501600102
State	Published - 4 Oct 2005

Keywords

Apoptosis
Glucose deprivation
Scaffold

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10.1073/pnas.0501600102

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Kim, J. W., Kim, M. J., Kim, K. J., Yun, H. J., Chae, J. S., Hwang, S. G., Chang, T. S., Park, H. S., Lee, K. W., Han, P. L., Cho, S. G., Kim, T. W., & Choi, E. J. (2005). Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway. Proceedings of the National Academy of Sciences of the United States of America, 102(40), 14308-14313. https://doi.org/10.1073/pnas.0501600102

@article{0558cdc0b75749dfaf243b0cfe049f21,

title = "Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway",

abstract = "The transmembrane protein Notch is cleaved by γ-secretase to yield an active form. Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.",

keywords = "Apoptosis, Glucose deprivation, Scaffold",

author = "Kim, {Jin Woo} and Kim, {Myung Jin} and Kim, {Kwang Je} and Yun, {Hee Jae} and Chae, {Ji Soo} and Hwang, {Sang Gil} and Chang, {Tong Shin} and Park, {Hee Sae} and Lee, {Kang Woo} and Han, {Pyung Lim} and Cho, {Ssang Goo} and Kim, {Tae Wan} and Choi, {Eui Ju}",

year = "2005",

month = oct,

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doi = "10.1073/pnas.0501600102",

language = "English",

volume = "102",

pages = "14308--14313",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

issn = "0027-8424",

publisher = "National Academy of Sciences",

number = "40",

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Kim, JW, Kim, MJ, Kim, KJ, Yun, HJ, Chae, JS, Hwang, SG, Chang, TS, Park, HS, Lee, KW, Han, PL, Cho, SG, Kim, TW & Choi, EJ 2005, 'Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway', Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 40, pp. 14308-14313. https://doi.org/10.1073/pnas.0501600102

TY - JOUR

T1 - Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

AU - Kim, Jin Woo

AU - Kim, Myung Jin

AU - Kim, Kwang Je

AU - Yun, Hee Jae

AU - Chae, Ji Soo

AU - Hwang, Sang Gil

AU - Chang, Tong Shin

AU - Park, Hee Sae

AU - Lee, Kang Woo

AU - Han, Pyung Lim

AU - Cho, Ssang Goo

AU - Kim, Tae Wan

AU - Choi, Eui Ju

PY - 2005/10/4

Y1 - 2005/10/4

N2 - The transmembrane protein Notch is cleaved by γ-secretase to yield an active form. Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.

AB - The transmembrane protein Notch is cleaved by γ-secretase to yield an active form. Notch intracellular domain (Notch-IC), in response to the binding of ligands, such as Jagged. Notch-IC contributes to the regulation of a variety of cellular events, including cell fate determination during embryonic development as well as cell growth, differentiation, and survival. We now show that Notch1-IC suppresses the scaffold activity of c-Jun N-terminal kinase (JNK)-interacting protein 1 (JIP1) in the JNK signaling pathway. Notch1-IC physically associated with the JNK binding domain of JIP1 and thereby interfered with the interaction between JIP1 and JNK. JIP1 mediated the activation of JNK1 induced by glucose deprivation in mouse embryonic fibroblasts, and ectopic expression of Notch1-IC inhibited JNK activation and apoptosis triggered by glucose deprivation. Taken together, these findings suggest that Notch1-IC negatively regulates the JNK pathway by disrupting the scaffold function of JIP1.

KW - Apoptosis

KW - Glucose deprivation

KW - Scaffold

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U2 - 10.1073/pnas.0501600102

DO - 10.1073/pnas.0501600102

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AN - SCOPUS:26444435322

SN - 0027-8424

VL - 102

SP - 14308

EP - 14313

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 40

ER -

Notch interferes with the scaffold function of JNK-interacting protein 1 to inhibit the JNK signaling pathway

Abstract

Keywords

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