An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

Kelly Velasco; Bin Zhao; Simone Callegari; Mikael Altun; Haiyin Liu; Gerco Hassink; Maria G. Masucci; Kristina Lindsten

doi:10.1016/j.bbrc.2013.02.094

An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

Kelly Velasco
, Bin Zhao
, Simone Callegari
, Mikael Altun
, Haiyin Liu
, Gerco Hassink
, Maria G. Masucci^*
, Kristina Lindsten^*

^*Corresponding author for this work

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

13 Citations (Scopus)

Abstract

The Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases.

Original language	English
Pages (from-to)	390-395
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	433
Issue number	4
Early online date	13 Mar 2013
DOIs	https://doi.org/10.1016/j.bbrc.2013.02.094
Publication status	Published - 19 Apr 2013
Externally published	Yes

Keywords

Proteasomal degradation
SIAH degron
SIAH1 ligase
USP19

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10.1016/j.bbrc.2013.02.094

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title = "An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19",

abstract = "The Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases.",

keywords = "Proteasomal degradation, SIAH degron, SIAH1 ligase, USP19",

author = "Kelly Velasco and Bin Zhao and Simone Callegari and Mikael Altun and Haiyin Liu and Gerco Hassink and Masucci, \{Maria G.\} and Kristina Lindsten",

note = "Funding Information: We thank Ze{\textquoteright}ev Ronai, Solomon H. Snyder and Chris Pugh for the kind gift of plasmids and reagents. This work was sponsored by awarded by Karolinska Institutet (to K.L, M.A, B.Z), {\AA}ke Wibergs Stiftelse (to K.L, M.A), the Swedish Research Council (to K.L), Magnus Bergvalls Stiftelse (to K.L, M.A) and ERACOL (to K.V.).",

year = "2013",

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doi = "10.1016/j.bbrc.2013.02.094",

language = "English",

volume = "433",

pages = "390--395",

journal = "Biochemical and biophysical research communications",

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T1 - An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

AU - Velasco, Kelly

AU - Zhao, Bin

AU - Callegari, Simone

AU - Altun, Mikael

AU - Liu, Haiyin

AU - Hassink, Gerco

AU - Masucci, Maria G.

AU - Lindsten, Kristina

N1 - Funding Information: We thank Ze’ev Ronai, Solomon H. Snyder and Chris Pugh for the kind gift of plasmids and reagents. This work was sponsored by awarded by Karolinska Institutet (to K.L, M.A, B.Z), Åke Wibergs Stiftelse (to K.L, M.A), the Swedish Research Council (to K.L), Magnus Bergvalls Stiftelse (to K.L, M.A) and ERACOL (to K.V.).

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N2 - The Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases.

AB - The Ubiquitin Specific Protease-19 (USP19) regulates cell cycle progression and is involved in the cellular response to different types of stress, including the unfolded protein response (UPR), hypoxia and muscle atrophy. Using the unique N-terminal domain as bait in a yeast-two hybrid screen we have identified the ubiquitin ligases Seven In Absentia Homolog (SIAH)-1 and SIAH2 as binding partners of USP19. The interaction is mediated by a SIAH-consensus binding motif and promotes USP19 ubiquitylation and proteasome-dependent degradation. These findings identify USP19 as a common substrate of the SIAH ubiquitin ligases.

KW - Proteasomal degradation

KW - SIAH degron

KW - SIAH1 ligase

KW - USP19

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DO - 10.1016/j.bbrc.2013.02.094

M3 - Article

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AN - SCOPUS:84876466143

SN - 0006-291X

VL - 433

SP - 390

EP - 395

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 4

ER -

An N-terminal SIAH-interacting motif regulates the stability of the ubiquitin specific protease (USP)-19

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Keywords

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