Regulation of catalytic activities of HECT ubiquitin ligases

Younghoon Kee; Jon M. Huibregtse

doi:10.1016/j.bbrc.2007.01.025

Regulation of catalytic activities of HECT ubiquitin ligases

Younghoon Kee, Jon M. Huibregtse

Department of New Biology

University of Texas at Austin

Research output: Contribution to journal › Short survey › peer-review

91 Scopus citations

Abstract

Studies in yeast and mammalian cells over the past decade have shown that HECT domain ubiquitin ligases (HECT E3 enzymes) are involved in diverse physiological pathways. Many substrates of specific HECT E3s have been identified, as well as many adaptor proteins that aid in defining substrate specificity or intra-cellular localization of HECT E3s. Here we review some recently discovered mechanisms for regulation of the catalytic activities of HECT E3s, including regulation at the level of E2 recruitment, phosphorylation-dependent relief of inhibitory intra-molecular interactions, and regulation by association with a deubiquitinating enzyme.

Original language	English
Pages (from-to)	329-333
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	354
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2007.01.025
State	Published - 9 Mar 2007

Bibliographical note

Funding Information:
We thank members of the Huibregtse lab for helpful discussions. This work was supported by the Institute for Cellular and Molecular Biology at the University of Texas at Austin and a grant to J.M.H. from the National Institutes of Health (CA072943).

Keywords

HECT ubiquitin ligases
Itch
Rsp5
Smurf2
Ubiquitin

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10.1016/j.bbrc.2007.01.025

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title = "Regulation of catalytic activities of HECT ubiquitin ligases",

abstract = "Studies in yeast and mammalian cells over the past decade have shown that HECT domain ubiquitin ligases (HECT E3 enzymes) are involved in diverse physiological pathways. Many substrates of specific HECT E3s have been identified, as well as many adaptor proteins that aid in defining substrate specificity or intra-cellular localization of HECT E3s. Here we review some recently discovered mechanisms for regulation of the catalytic activities of HECT E3s, including regulation at the level of E2 recruitment, phosphorylation-dependent relief of inhibitory intra-molecular interactions, and regulation by association with a deubiquitinating enzyme.",

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note = "Funding Information: We thank members of the Huibregtse lab for helpful discussions. This work was supported by the Institute for Cellular and Molecular Biology at the University of Texas at Austin and a grant to J.M.H. from the National Institutes of Health (CA072943).",

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doi = "10.1016/j.bbrc.2007.01.025",

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T1 - Regulation of catalytic activities of HECT ubiquitin ligases

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AU - Huibregtse, Jon M.

N1 - Funding Information: We thank members of the Huibregtse lab for helpful discussions. This work was supported by the Institute for Cellular and Molecular Biology at the University of Texas at Austin and a grant to J.M.H. from the National Institutes of Health (CA072943).

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N2 - Studies in yeast and mammalian cells over the past decade have shown that HECT domain ubiquitin ligases (HECT E3 enzymes) are involved in diverse physiological pathways. Many substrates of specific HECT E3s have been identified, as well as many adaptor proteins that aid in defining substrate specificity or intra-cellular localization of HECT E3s. Here we review some recently discovered mechanisms for regulation of the catalytic activities of HECT E3s, including regulation at the level of E2 recruitment, phosphorylation-dependent relief of inhibitory intra-molecular interactions, and regulation by association with a deubiquitinating enzyme.

AB - Studies in yeast and mammalian cells over the past decade have shown that HECT domain ubiquitin ligases (HECT E3 enzymes) are involved in diverse physiological pathways. Many substrates of specific HECT E3s have been identified, as well as many adaptor proteins that aid in defining substrate specificity or intra-cellular localization of HECT E3s. Here we review some recently discovered mechanisms for regulation of the catalytic activities of HECT E3s, including regulation at the level of E2 recruitment, phosphorylation-dependent relief of inhibitory intra-molecular interactions, and regulation by association with a deubiquitinating enzyme.

KW - HECT ubiquitin ligases

KW - Itch

KW - Rsp5

KW - Smurf2

KW - Ubiquitin

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AN - SCOPUS:33846497347

SN - 0006-291X

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SP - 329

EP - 333

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Regulation of catalytic activities of HECT ubiquitin ligases

Abstract

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Keywords

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