CDIP1-BAP31 Complex Transduces Apoptotic Signals from Endoplasmic Reticulum to Mitochondria under Endoplasmic Reticulum Stress

Takushi Namba; Fang Tian; Kiki Chu; So Young Hwang; Kyoung Wan Yoon; Sanguine Byun; Masatsugu Hiraki; Anna Mandinova; Sam W. Lee

doi:10.1016/j.celrep.2013.09.020

CDIP1-BAP31 Complex Transduces Apoptotic Signals from Endoplasmic Reticulum to Mitochondria under Endoplasmic Reticulum Stress

Takushi Namba, Fang Tian, Kiki Chu, So Young Hwang, Kyoung Wan Yoon, Sanguine Byun, Masatsugu Hiraki, Anna Mandinova, Sam W. Lee

Division of Life Sciences

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

70 Citations (Scopus)

Abstract

Resolved endoplasmic reticulum (ER) stress response is essential for intracellular homeostatic balance, but unsettled ER stress can lead to apoptosis. Here, we show that a proapoptotic p53 target, CDIP1, acts as a key signal transducer of ER-stress-mediated apoptosis. We identify B-cell-receptor-associated protein 31 (BAP31) as an interacting partner of CDIP1. Upon ER stress, CDIP1 is induced and enhances an association with BAP31 at the ER membrane. We also show that CDIP1 binding to BAP31 is required for BAP31 cleavage upon ER stress and for BAP31-Bcl-2 association. The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization. Genetic knockout of CDIP1 in mice leads to impaired response to ER-stress-mediated apoptosis. Altogether, our data demonstrate that the CDIP1/BAP31-mediated regulation of mitochondrial apoptosis pathway represents a mechanism for establishing an ER-mitochondrial crosstalk for ER-stress-mediated apoptosis signaling

Original language	English
Pages (from-to)	331-339
Number of pages	9
Journal	Cell Reports
Volume	5
Issue number	2
DOIs	https://doi.org/10.1016/j.celrep.2013.09.020
Publication status	Published - 2013

Bibliographical note

Funding Information:
LC-MS/MS analysis was performed by the Taplin Biological Mass Spectrometry Facility of Harvard Medical School. We thank S. Aaronson for helpful advice and suggestions during the project. This work was partially supported by National Institutes of Health grants CA142805, CA080058, and CA127247. T.N. was supported by a fellowship for research abroad from Japan Society for the Promotion of Science and is a recipient of an AACR-Bristol-Myers Squibb Oncology Scholar-in-Training grant. S.-Y.H. was supported by the Korean Government Research Foundation (KRF-2008-357-E00023).

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/j.celrep.2013.09.020

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@article{34235e3d1c2d4b10b0eeb06d3b10d2cd,

title = "CDIP1-BAP31 Complex Transduces Apoptotic Signals from Endoplasmic Reticulum to Mitochondria under Endoplasmic Reticulum Stress",

abstract = "Resolved endoplasmic reticulum (ER) stress response is essential for intracellular homeostatic balance, but unsettled ER stress can lead to apoptosis. Here, we show that a proapoptotic p53 target, CDIP1, acts as a key signal transducer of ER-stress-mediated apoptosis. We identify B-cell-receptor-associated protein 31 (BAP31) as an interacting partner of CDIP1. Upon ER stress, CDIP1 is induced and enhances an association with BAP31 at the ER membrane. We also show that CDIP1 binding to BAP31 is required for BAP31 cleavage upon ER stress and for BAP31-Bcl-2 association. The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization. Genetic knockout of CDIP1 in mice leads to impaired response to ER-stress-mediated apoptosis. Altogether, our data demonstrate that the CDIP1/BAP31-mediated regulation of mitochondrial apoptosis pathway represents a mechanism for establishing an ER-mitochondrial crosstalk for ER-stress-mediated apoptosis signaling",

author = "Takushi Namba and Fang Tian and Kiki Chu and Hwang, {So Young} and Yoon, {Kyoung Wan} and Sanguine Byun and Masatsugu Hiraki and Anna Mandinova and Lee, {Sam W.}",

note = "Funding Information: LC-MS/MS analysis was performed by the Taplin Biological Mass Spectrometry Facility of Harvard Medical School. We thank S. Aaronson for helpful advice and suggestions during the project. This work was partially supported by National Institutes of Health grants CA142805, CA080058, and CA127247. T.N. was supported by a fellowship for research abroad from Japan Society for the Promotion of Science and is a recipient of an AACR-Bristol-Myers Squibb Oncology Scholar-in-Training grant. S.-Y.H. was supported by the Korean Government Research Foundation (KRF-2008-357-E00023). ",

year = "2013",

doi = "10.1016/j.celrep.2013.09.020",

language = "English",

volume = "5",

pages = "331--339",

journal = "Cell Reports",

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T1 - CDIP1-BAP31 Complex Transduces Apoptotic Signals from Endoplasmic Reticulum to Mitochondria under Endoplasmic Reticulum Stress

AU - Namba, Takushi

AU - Tian, Fang

AU - Chu, Kiki

AU - Hwang, So Young

AU - Yoon, Kyoung Wan

AU - Byun, Sanguine

AU - Hiraki, Masatsugu

AU - Mandinova, Anna

AU - Lee, Sam W.

N1 - Funding Information: LC-MS/MS analysis was performed by the Taplin Biological Mass Spectrometry Facility of Harvard Medical School. We thank S. Aaronson for helpful advice and suggestions during the project. This work was partially supported by National Institutes of Health grants CA142805, CA080058, and CA127247. T.N. was supported by a fellowship for research abroad from Japan Society for the Promotion of Science and is a recipient of an AACR-Bristol-Myers Squibb Oncology Scholar-in-Training grant. S.-Y.H. was supported by the Korean Government Research Foundation (KRF-2008-357-E00023).

PY - 2013

Y1 - 2013

N2 - Resolved endoplasmic reticulum (ER) stress response is essential for intracellular homeostatic balance, but unsettled ER stress can lead to apoptosis. Here, we show that a proapoptotic p53 target, CDIP1, acts as a key signal transducer of ER-stress-mediated apoptosis. We identify B-cell-receptor-associated protein 31 (BAP31) as an interacting partner of CDIP1. Upon ER stress, CDIP1 is induced and enhances an association with BAP31 at the ER membrane. We also show that CDIP1 binding to BAP31 is required for BAP31 cleavage upon ER stress and for BAP31-Bcl-2 association. The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization. Genetic knockout of CDIP1 in mice leads to impaired response to ER-stress-mediated apoptosis. Altogether, our data demonstrate that the CDIP1/BAP31-mediated regulation of mitochondrial apoptosis pathway represents a mechanism for establishing an ER-mitochondrial crosstalk for ER-stress-mediated apoptosis signaling

AB - Resolved endoplasmic reticulum (ER) stress response is essential for intracellular homeostatic balance, but unsettled ER stress can lead to apoptosis. Here, we show that a proapoptotic p53 target, CDIP1, acts as a key signal transducer of ER-stress-mediated apoptosis. We identify B-cell-receptor-associated protein 31 (BAP31) as an interacting partner of CDIP1. Upon ER stress, CDIP1 is induced and enhances an association with BAP31 at the ER membrane. We also show that CDIP1 binding to BAP31 is required for BAP31 cleavage upon ER stress and for BAP31-Bcl-2 association. The recruitment of Bcl-2 to the BAP31-CDIP1 complex, as well as CDIP1-dependent truncated Bid (tBid) and caspase-8 activation, contributes to BAX oligomerization. Genetic knockout of CDIP1 in mice leads to impaired response to ER-stress-mediated apoptosis. Altogether, our data demonstrate that the CDIP1/BAP31-mediated regulation of mitochondrial apoptosis pathway represents a mechanism for establishing an ER-mitochondrial crosstalk for ER-stress-mediated apoptosis signaling

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ER -

CDIP1-BAP31 Complex Transduces Apoptotic Signals from Endoplasmic Reticulum to Mitochondria under Endoplasmic Reticulum Stress

Abstract

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