K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

Wei Chien Yuan; Yu Ru Lee; Shu Yu Lin; Li Ying Chang; Yen Pei Tan; Chin Chun Hung; Jean Cheng Kuo; Cheng Hsin Liu; Mei Yao Lin; Ming Xu; Zhijian J. Chen; Ruey Hwa Chen

doi:10.1016/j.molcel.2014.03.035

K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

Wei Chien Yuan, Yu Ru Lee, Shu Yu Lin, Li Ying Chang, Yen Pei Tan, Chin Chun Hung, Jean Cheng Kuo, Cheng Hsin Liu, Mei Yao Lin, Ming Xu, Zhijian J. Chen, Ruey Hwa Chen

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126 Scopus citations

Abstract

Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.

Original language	English (US)
Pages (from-to)	586-600
Number of pages	15
Journal	Molecular cell
Volume	54
Issue number	4
DOIs	https://doi.org/10.1016/j.molcel.2014.03.035
State	Published - May 22 2014

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2014.03.035

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@article{c2c582ab5aac402892fbd686bb81cbf3,

title = "K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking",

abstract = "Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.",

author = "Yuan, {Wei Chien} and Lee, {Yu Ru} and Lin, {Shu Yu} and Chang, {Li Ying} and Tan, {Yen Pei} and Hung, {Chin Chun} and Kuo, {Jean Cheng} and Liu, {Cheng Hsin} and Lin, {Mei Yao} and Ming Xu and Chen, {Zhijian J.} and Chen, {Ruey Hwa}",

note = "Funding Information: We thank Jennifer Lippincott-Schwartz, Ludger Johannes, Satoshi Waguri, Guang-Chao Chen, Sandra Schmid, Angelika A. Noegel, Tamas Balla, Geri Kreitzer, Lih-Hwa Hwang, and Robin F. Irvine for constructs; the National RNAi Core Facility for shRNA constructs; the Academia Sinica Mass Spectrometry Facility for LC-MS/MS analysis; and Fang-Jen Lee and Ming-Daw Tsai for discussion. This work was supported by NSC Frontier Grant 101-2321-B-001-007 and by the Academia Sinica Investigator Award. ",

year = "2014",

month = may,

day = "22",

doi = "10.1016/j.molcel.2014.03.035",

language = "English (US)",

volume = "54",

pages = "586--600",

journal = "Molecular cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "4",

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TY - JOUR

T1 - K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

AU - Yuan, Wei Chien

AU - Lee, Yu Ru

AU - Lin, Shu Yu

AU - Chang, Li Ying

AU - Tan, Yen Pei

AU - Hung, Chin Chun

AU - Kuo, Jean Cheng

AU - Liu, Cheng Hsin

AU - Lin, Mei Yao

AU - Xu, Ming

AU - Chen, Zhijian J.

AU - Chen, Ruey Hwa

N1 - Funding Information: We thank Jennifer Lippincott-Schwartz, Ludger Johannes, Satoshi Waguri, Guang-Chao Chen, Sandra Schmid, Angelika A. Noegel, Tamas Balla, Geri Kreitzer, Lih-Hwa Hwang, and Robin F. Irvine for constructs; the National RNAi Core Facility for shRNA constructs; the Academia Sinica Mass Spectrometry Facility for LC-MS/MS analysis; and Fang-Jen Lee and Ming-Daw Tsai for discussion. This work was supported by NSC Frontier Grant 101-2321-B-001-007 and by the Academia Sinica Investigator Award.

PY - 2014/5/22

Y1 - 2014/5/22

N2 - Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.

AB - Ubiquitin chains are formed as structurally distinct polymers via different linkages, and several chain types including K33-linkage remain uncharacterized. Here, we describe a role for K33-polyubiquitination in protein trafficking. We show that the Cullin 3 (Cul3) substrate adaptor KLHL20 is localized to the trans-Golgi network (TGN) and is important for post-Golgi trafficking by promoting the biogenesis of TGN-derived transport carriers. The Cul3-KLHL20 ubiquitin E3 ligase catalyzes a nondegradable, K33-linked polyubiquitination on coronin 7 (Crn7), which facilitates Crn7 targeting to TGN through a ubiquitin-dependent interaction with Eps15. Blockage of K33-chain formation, Crn7 ubiquitination, or disruption of Crn7-Eps15 interaction impairs TGN-pool F-actin assembly, a process essential for generating transport carriers. Enforced targeting of Crn7 to TGN bypasses the requirement of K33-ubiquitination for TGN-pool F-actin assembly and post-Golgi trafficking. Our study reveals a role of KLHL20-mediated K33-ubiquitination of Crn7 in post-Golgi transport and identifies a cellular recognition mechanism for this ubiquitin chain type.

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U2 - 10.1016/j.molcel.2014.03.035

DO - 10.1016/j.molcel.2014.03.035

M3 - Article

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AN - SCOPUS:84901004245

SN - 1097-2765

VL - 54

SP - 586

EP - 600

JO - Molecular cell

JF - Molecular cell

IS - 4

ER -

K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

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