Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins

Sun Mi Park; Shimin Hu; Tae H. Lee; Xiaolu Yang

doi:10.1016/S0076-6879(08)01613-3

Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins

Sun Mi Park, Shimin Hu, Tae H. Lee, Xiaolu Yang

Department of System Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Inhibitor of apoptosis (IAP) proteins are a family of evolutionarily conserved proteins that regulate apoptosis as well as other cellular processes. The functions of many IAPs are defined by their RING domains, which possess E3 ubiquitin ligase activity and promote proteasomal degradation of an increasing number of target proteins. In this chapter, we describe the methods used in our laboratories to study the IAP's E3 activity.

Original language	English
Title of host publication	Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B
Editors	Roya Khosravi-Far, Zahra Zakeri, Richard Lockshin, Mauro Piacentini
Pages	225-235
Number of pages	11
DOIs	https://doi.org/10.1016/S0076-6879(08)01613-3
Publication status	Published - 2008

Publication series

Name	Methods in Enzymology
Volume	446
ISSN (Print)	0076-6879

Bibliographical note

Funding Information:
This work was supported by NIH grants CA88868 and CA108872 and a Leukemia & Lymphoma Society Scholar award to X. Y., and the Korea Research Foundation Grant (KRF‐2006‐005‐J04502) and Brain Korea 21 project to T.H.L. The authors are grateful for critical reading of the manuscript by the members of the Yang laboratory.

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

Access to Document

10.1016/S0076-6879(08)01613-3

Cite this

Park, S. M., Hu, S., Lee, T. H., & Yang, X. (2008). Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins. In R. Khosravi-Far, Z. Zakeri, R. Lockshin, & M. Piacentini (Eds.), Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B (pp. 225-235). (Methods in Enzymology; Vol. 446). https://doi.org/10.1016/S0076-6879(08)01613-3

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title = "Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins",

abstract = "Inhibitor of apoptosis (IAP) proteins are a family of evolutionarily conserved proteins that regulate apoptosis as well as other cellular processes. The functions of many IAPs are defined by their RING domains, which possess E3 ubiquitin ligase activity and promote proteasomal degradation of an increasing number of target proteins. In this chapter, we describe the methods used in our laboratories to study the IAP's E3 activity.",

author = "Park, {Sun Mi} and Shimin Hu and Lee, {Tae H.} and Xiaolu Yang",

note = "Funding Information: This work was supported by NIH grants CA88868 and CA108872 and a Leukemia & Lymphoma Society Scholar award to X. Y., and the Korea Research Foundation Grant (KRF‐2006‐005‐J04502) and Brain Korea 21 project to T.H.L. The authors are grateful for critical reading of the manuscript by the members of the Yang laboratory.",

year = "2008",

doi = "10.1016/S0076-6879(08)01613-3",

language = "English",

isbn = "9780123744647",

series = "Methods in Enzymology",

pages = "225--235",

editor = "Roya Khosravi-Far and Zahra Zakeri and Richard Lockshin and Mauro Piacentini",

booktitle = "Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B",

}

Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins. / Park, Sun Mi; Hu, Shimin; Lee, Tae H. et al.
Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B. ed. / Roya Khosravi-Far; Zahra Zakeri; Richard Lockshin; Mauro Piacentini. 2008. p. 225-235 (Methods in Enzymology; Vol. 446).

Research output: Chapter in Book/Report/Conference proceeding › Chapter

TY - CHAP

T1 - Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins

AU - Park, Sun Mi

AU - Hu, Shimin

AU - Lee, Tae H.

AU - Yang, Xiaolu

N1 - Funding Information: This work was supported by NIH grants CA88868 and CA108872 and a Leukemia & Lymphoma Society Scholar award to X. Y., and the Korea Research Foundation Grant (KRF‐2006‐005‐J04502) and Brain Korea 21 project to T.H.L. The authors are grateful for critical reading of the manuscript by the members of the Yang laboratory.

PY - 2008

Y1 - 2008

N2 - Inhibitor of apoptosis (IAP) proteins are a family of evolutionarily conserved proteins that regulate apoptosis as well as other cellular processes. The functions of many IAPs are defined by their RING domains, which possess E3 ubiquitin ligase activity and promote proteasomal degradation of an increasing number of target proteins. In this chapter, we describe the methods used in our laboratories to study the IAP's E3 activity.

AB - Inhibitor of apoptosis (IAP) proteins are a family of evolutionarily conserved proteins that regulate apoptosis as well as other cellular processes. The functions of many IAPs are defined by their RING domains, which possess E3 ubiquitin ligase activity and promote proteasomal degradation of an increasing number of target proteins. In this chapter, we describe the methods used in our laboratories to study the IAP's E3 activity.

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SN - 9780123744647

T3 - Methods in Enzymology

SP - 225

EP - 235

BT - Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B

A2 - Khosravi-Far, Roya

A2 - Zakeri, Zahra

A2 - Lockshin, Richard

A2 - Piacentini, Mauro

ER -

Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins

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Bibliographical note

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