Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast

Takeshi Sekiguchi; Toru Sasaki; Minoru Funakoshi; Takashi Ishii; Yoh hei Saitoh; Shu ichi Kaneko; Hideki Kobayashi

doi:10.1016/j.bbrc.2011.06.183

Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast

Takeshi Sekiguchi, Toru Sasaki, Minoru Funakoshi, Takashi Ishii, Yoh hei Saitoh, Shu ichi Kaneko, Hideki Kobayashi

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

4 Citations (Scopus)

Abstract

Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2Δ. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.

Original language	English
Pages (from-to)	555-561
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	411
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2011.06.183
Publication status	Published - Aug 5 2011
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2011.06.183

Cite this

@article{6825af871bef4bd29ae343bfdcb3102a,

title = "Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast",

abstract = "Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2Δ. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.",

author = "Takeshi Sekiguchi and Toru Sasaki and Minoru Funakoshi and Takashi Ishii and Saitoh, {Yoh hei} and Kaneko, {Shu ichi} and Hideki Kobayashi",

note = "Funding Information: This work was supported by grants from the Ministry of Education, Science, Sports, and Technology of Japan, and by CREST, JST Japan. ",

year = "2011",

month = aug,

day = "5",

doi = "10.1016/j.bbrc.2011.06.183",

language = "English",

volume = "411",

pages = "555--561",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast

AU - Sekiguchi, Takeshi

AU - Sasaki, Toru

AU - Funakoshi, Minoru

AU - Ishii, Takashi

AU - Saitoh, Yoh hei

AU - Kaneko, Shu ichi

AU - Kobayashi, Hideki

N1 - Funding Information: This work was supported by grants from the Ministry of Education, Science, Sports, and Technology of Japan, and by CREST, JST Japan.

PY - 2011/8/5

Y1 - 2011/8/5

N2 - Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2Δ. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.

AB - Ubiquitin-like (UBL)-ubiquitin-associated (UBA) proteins, including Dsk2 and Rad23, act as delivery factors that target polyubiquitinated substrates to the proteasome. We report here that the Dsk2 UBL domain is ubiquitinated in yeast cells and that Dsk2 ubiquitination of the UBL domain is involved in Dsk2 stability, depending on the Dsk2 UBA domain. Also, Dsk2 lacking ubiquitin chains impaired ubiquitin-dependent protein degradation and decreased the interaction of Dsk2 with polyubiquitinated proteins in cells. Moreover, Dsk2 ubiquitination affected ability to restore the temperature-sensitive growth defect of dsk2Δ. These results indicate that ubiquitination in the UBL domain of Dsk2 has in vivo functions in the ubiquitin-proteasome pathway in yeast.

UR - http://www.scopus.com/inward/record.url?scp=79961126998&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79961126998&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2011.06.183

DO - 10.1016/j.bbrc.2011.06.183

M3 - Article

C2 - 21763274

AN - SCOPUS:79961126998

SN - 0006-291X

VL - 411

SP - 555

EP - 561

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this