Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6

Wissam Mansour; Mark A. Nakasone; Maximilian Von Delbrück; Zanlin Yu; Daria Krutauz; Noa Reis; Oded Kleifeld; Thomas Sommer; David Fushman; Michael H. Glickman

doi:10.1074/jbc.M114.568295

Disassembly of Lys₁₁ and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6

Wissam Mansour, Mark A. Nakasone, Maximilian Von Delbrück, Zanlin Yu, Daria Krutauz, Noa Reis, Oded Kleifeld, Thomas Sommer, David Fushman, Michael H. Glickman

Biology

Technion - Israel Institute of Technology

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

Abstract

Background: Deconjugation of polyubiquitin is an essential step in preparing substrates for proteolysis by the 26S proteasome. Results: Proteasome-associated DUBs, Rpn11 and Ubp6, process long Lys₁₁- or Lys₆₃-linked polyUb more efficiently than Lys₄₈ linkages. Conclusion: 26S proteasomes can completely disassemble a mixed/branched polyUb conjugate. Significance: These observations call into question what constitutes an efficient signal for proteasome targeting versus proteolysis.

Original language	English
Pages (from-to)	4688-4704
Number of pages	17
Journal	Journal of Biological Chemistry
Volume	290
Issue number	8
DOIs	https://doi.org/10.1074/jbc.M114.568295
State	Published - 20 Feb 2015

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M114.568295

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Mansour, W., Nakasone, M. A., Von Delbrück, M., Yu, Z., Krutauz, D., Reis, N., Kleifeld, O., Sommer, T., Fushman, D., & Glickman, M. H. (2015). Disassembly of Lys₁₁ and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6. Journal of Biological Chemistry, 290(8), 4688-4704. https://doi.org/10.1074/jbc.M114.568295

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title = "Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6",

abstract = "Background: Deconjugation of polyubiquitin is an essential step in preparing substrates for proteolysis by the 26S proteasome. Results: Proteasome-associated DUBs, Rpn11 and Ubp6, process long Lys11- or Lys63-linked polyUb more efficiently than Lys48 linkages. Conclusion: 26S proteasomes can completely disassemble a mixed/branched polyUb conjugate. Significance: These observations call into question what constitutes an efficient signal for proteasome targeting versus proteolysis.",

author = "Wissam Mansour and Nakasone, \{Mark A.\} and \{Von Delbr{\"u}ck\}, Maximilian and Zanlin Yu and Daria Krutauz and Noa Reis and Oded Kleifeld and Thomas Sommer and David Fushman and Glickman, \{Michael H.\}",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

month = feb,

day = "20",

doi = "10.1074/jbc.M114.568295",

language = "الإنجليزيّة",

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Mansour, W, Nakasone, MA, Von Delbrück, M, Yu, Z, Krutauz, D, Reis, N, Kleifeld, O, Sommer, T, Fushman, D & Glickman, MH 2015, 'Disassembly of Lys₁₁ and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6', Journal of Biological Chemistry, vol. 290, no. 8, pp. 4688-4704. https://doi.org/10.1074/jbc.M114.568295

TY - JOUR

T1 - Disassembly of Lys11 and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6

AU - Mansour, Wissam

AU - Nakasone, Mark A.

AU - Von Delbrück, Maximilian

AU - Yu, Zanlin

AU - Krutauz, Daria

AU - Reis, Noa

AU - Kleifeld, Oded

AU - Sommer, Thomas

AU - Fushman, David

AU - Glickman, Michael H.

PY - 2015/2/20

Y1 - 2015/2/20

N2 - Background: Deconjugation of polyubiquitin is an essential step in preparing substrates for proteolysis by the 26S proteasome. Results: Proteasome-associated DUBs, Rpn11 and Ubp6, process long Lys11- or Lys63-linked polyUb more efficiently than Lys48 linkages. Conclusion: 26S proteasomes can completely disassemble a mixed/branched polyUb conjugate. Significance: These observations call into question what constitutes an efficient signal for proteasome targeting versus proteolysis.

AB - Background: Deconjugation of polyubiquitin is an essential step in preparing substrates for proteolysis by the 26S proteasome. Results: Proteasome-associated DUBs, Rpn11 and Ubp6, process long Lys11- or Lys63-linked polyUb more efficiently than Lys48 linkages. Conclusion: 26S proteasomes can completely disassemble a mixed/branched polyUb conjugate. Significance: These observations call into question what constitutes an efficient signal for proteasome targeting versus proteolysis.

UR - http://www.scopus.com/inward/record.url?scp=84928712769&partnerID=8YFLogxK

U2 - 10.1074/jbc.M114.568295

DO - 10.1074/jbc.M114.568295

M3 - مقالة

SN - 0021-9258

VL - 290

SP - 4688

EP - 4704

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 8

ER -

Disassembly of Lys₁₁ and mixed linkage polyubiquitin conjugates provides insights into function of proteasomal deubiquitinases Rpn11 and Ubp6

Abstract

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