Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase

Kenji Ishimoto; Ayaka Hayase; Fumiko Kumagai; Megumi Kawai; Hiroko Okuno; Nobumasa Hino; Yoshiaki Okada; Takeshi Kawamura; Toshiya Tanaka; Takao Hamakubo; Juro Sakai; Tatsuhiko Kodama; Keisuke Tachibana; Takefumi Doi

doi:10.1016/j.bbrc.2017.04.159

Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase

Kenji Ishimoto, Ayaka Hayase, Fumiko Kumagai, Megumi Kawai, Hiroko Okuno, Nobumasa Hino, Yoshiaki Okada, Takeshi Kawamura, Toshiya Tanaka, Takao Hamakubo, Juro Sakai, Tatsuhiko Kodama, Keisuke Tachibana, Takefumi Doi

MED - Medical Sciences

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

6 Citations (Scopus)

Abstract

Lipin-1 has dual functions in the regulation of lipid and energy metabolism according to its subcellular localization, which is tightly controlled. However, it is unclear how Lipin-1 degradation is regulated. Here, we demonstrate that Lipin-1 is degraded through its DSGXXS motif. We show that Lipin-1 interacts with either of two E3 ubiquitin ligases, BTRC or FBXW11, and that this interaction is DSGXXS-dependent and mediates the attachment of polyubiquitin chains. Further, we demonstrate that degradation of Lipin-1 is regulated by BTRC in the cytoplasm and on membranes. These novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes.

Original language	English
Pages (from-to)	159-164
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	488
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2017.04.159
Publication status	Published - 2017 Jun 17

Keywords

BTRC
Degradation
Lipid metabolism
Lipin-1
Polyubiquitination
Protein localization

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10.1016/j.bbrc.2017.04.159

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title = "Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase",

abstract = "Lipin-1 has dual functions in the regulation of lipid and energy metabolism according to its subcellular localization, which is tightly controlled. However, it is unclear how Lipin-1 degradation is regulated. Here, we demonstrate that Lipin-1 is degraded through its DSGXXS motif. We show that Lipin-1 interacts with either of two E3 ubiquitin ligases, BTRC or FBXW11, and that this interaction is DSGXXS-dependent and mediates the attachment of polyubiquitin chains. Further, we demonstrate that degradation of Lipin-1 is regulated by BTRC in the cytoplasm and on membranes. These novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes.",

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author = "Kenji Ishimoto and Ayaka Hayase and Fumiko Kumagai and Megumi Kawai and Hiroko Okuno and Nobumasa Hino and Yoshiaki Okada and Takeshi Kawamura and Toshiya Tanaka and Takao Hamakubo and Juro Sakai and Tatsuhiko Kodama and Keisuke Tachibana and Takefumi Doi",

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T1 - Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase

AU - Ishimoto, Kenji

AU - Hayase, Ayaka

AU - Kumagai, Fumiko

AU - Kawai, Megumi

AU - Okuno, Hiroko

AU - Hino, Nobumasa

AU - Okada, Yoshiaki

AU - Kawamura, Takeshi

AU - Tanaka, Toshiya

AU - Hamakubo, Takao

AU - Sakai, Juro

AU - Kodama, Tatsuhiko

AU - Tachibana, Keisuke

AU - Doi, Takefumi

PY - 2017/6/17

Y1 - 2017/6/17

N2 - Lipin-1 has dual functions in the regulation of lipid and energy metabolism according to its subcellular localization, which is tightly controlled. However, it is unclear how Lipin-1 degradation is regulated. Here, we demonstrate that Lipin-1 is degraded through its DSGXXS motif. We show that Lipin-1 interacts with either of two E3 ubiquitin ligases, BTRC or FBXW11, and that this interaction is DSGXXS-dependent and mediates the attachment of polyubiquitin chains. Further, we demonstrate that degradation of Lipin-1 is regulated by BTRC in the cytoplasm and on membranes. These novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes.

AB - Lipin-1 has dual functions in the regulation of lipid and energy metabolism according to its subcellular localization, which is tightly controlled. However, it is unclear how Lipin-1 degradation is regulated. Here, we demonstrate that Lipin-1 is degraded through its DSGXXS motif. We show that Lipin-1 interacts with either of two E3 ubiquitin ligases, BTRC or FBXW11, and that this interaction is DSGXXS-dependent and mediates the attachment of polyubiquitin chains. Further, we demonstrate that degradation of Lipin-1 is regulated by BTRC in the cytoplasm and on membranes. These novel insights into the regulation of human Lipin-1 stability will be useful in planning further studies to elucidate its metabolic processes.

KW - BTRC

KW - Degradation

KW - Lipid metabolism

KW - Lipin-1

KW - Polyubiquitination

KW - Protein localization

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AN - SCOPUS:85019156342

SN - 0006-291X

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SP - 159

EP - 164

JO - Biochemical and Biophysical Research Communications

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IS - 1

ER -

Degradation of human Lipin-1 by BTRC E3 ubiquitin ligase

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Keywords

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