A snapshot of ubiquitin chain elongation: Lysine 48-tetra-ubiquitin slows down ubiquitination

Jordan Kovacev; Kenneth Wu; Donald E. Spratt; Robert A. Chong; Chan Lee; Jaladhi Nayak; Gary S. Shaw; Zhen Qiang Pan

doi:10.1074/jbc.M113.530576

A snapshot of ubiquitin chain elongation: Lysine 48-tetra-ubiquitin slows down ubiquitination

Jordan Kovacev, Kenneth Wu, Donald E. Spratt, Robert A. Chong, Chan Lee, Jaladhi Nayak, Gary S. Shaw, Zhen Qiang Pan

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

8 Scopus citations

Abstract

Background: Polyubiquitin chains are signaling polypeptides altering the fate of substrates. Results: A Lys-48-ubiquitin chain of a length greater than four, but not its Lys-63 linkage counterparts, slowed the rate of additional ubiquitin conjugation. Conclusion: The ubiquitin chain length and linkage may impact kinetic rates of chain elongation. Significance: Our findings suggest a self-restraining mechanism that limits Lys-48-polyubiquitination.

Original language	English
Pages (from-to)	7068-7081
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	289
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M113.530576
State	Published - 7 Mar 2014

Access to Document

10.1074/jbc.M113.530576

Cite this

@article{ff70de2ed7234329a6e077203b225304,

title = "A snapshot of ubiquitin chain elongation: Lysine 48-tetra-ubiquitin slows down ubiquitination",

abstract = "Background: Polyubiquitin chains are signaling polypeptides altering the fate of substrates. Results: A Lys-48-ubiquitin chain of a length greater than four, but not its Lys-63 linkage counterparts, slowed the rate of additional ubiquitin conjugation. Conclusion: The ubiquitin chain length and linkage may impact kinetic rates of chain elongation. Significance: Our findings suggest a self-restraining mechanism that limits Lys-48-polyubiquitination.",

author = "Jordan Kovacev and Kenneth Wu and Spratt, {Donald E.} and Chong, {Robert A.} and Chan Lee and Jaladhi Nayak and Shaw, {Gary S.} and Pan, {Zhen Qiang}",

year = "2014",

month = mar,

day = "7",

doi = "10.1074/jbc.M113.530576",

language = "English",

volume = "289",

pages = "7068--7081",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "10",

}

TY - JOUR

T1 - A snapshot of ubiquitin chain elongation

T2 - Lysine 48-tetra-ubiquitin slows down ubiquitination

AU - Kovacev, Jordan

AU - Wu, Kenneth

AU - Spratt, Donald E.

AU - Chong, Robert A.

AU - Lee, Chan

AU - Nayak, Jaladhi

AU - Shaw, Gary S.

AU - Pan, Zhen Qiang

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Background: Polyubiquitin chains are signaling polypeptides altering the fate of substrates. Results: A Lys-48-ubiquitin chain of a length greater than four, but not its Lys-63 linkage counterparts, slowed the rate of additional ubiquitin conjugation. Conclusion: The ubiquitin chain length and linkage may impact kinetic rates of chain elongation. Significance: Our findings suggest a self-restraining mechanism that limits Lys-48-polyubiquitination.

AB - Background: Polyubiquitin chains are signaling polypeptides altering the fate of substrates. Results: A Lys-48-ubiquitin chain of a length greater than four, but not its Lys-63 linkage counterparts, slowed the rate of additional ubiquitin conjugation. Conclusion: The ubiquitin chain length and linkage may impact kinetic rates of chain elongation. Significance: Our findings suggest a self-restraining mechanism that limits Lys-48-polyubiquitination.

UR - http://www.scopus.com/inward/record.url?scp=84896763575&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.530576

DO - 10.1074/jbc.M113.530576

M3 - Article

C2 - 24464578

AN - SCOPUS:84896763575

SN - 0021-9258

VL - 289

SP - 7068

EP - 7081

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 10

ER -

A snapshot of ubiquitin chain elongation: Lysine 48-tetra-ubiquitin slows down ubiquitination

Abstract

Access to Document

Fingerprint

Cite this