Chemistry

Document Type

Article

Abstract

ITCH (aka Atrophin-1-interacting protein 4) is a prominent member of the NEDD4 HECT (Homologous to E6AP C-Terminus) E3 ubiquitin ligase family that regulates numerous cellular functions including inflammatory responses through T-cell activation, cell differentiation, and apoptosis. Known intracellular targets of ITCH-dependent ubiquitylation include receptor proteins, signaling molecules, and transcription factors. The HECT C-terminal lobe of ITCH contains the conserved catalytic cysteine required for the covalent attachment of ubiquitin onto a substrate and polyubiquitin chain assembly. We report here the complete experimentally determined 1 H, 13 C, and 15 N backbone and sidechain resonance assignments for the HECT C-terminal lobe of ITCH (residues 784–903) using heteronuclear, multidimensional NMR spectroscopy. These resonance assignments will be used in future NMR-based studies to examine the role of dynamics and conformational flexibility in HECT-dependent ubiquitylation as well as deciphering the structural and biochemical basis for polyubiquitin chain synthesis and specificity by ITCH.

Publication Title

Biomolecular NMR Assignments

Publication Date

4-2019

Volume

13

Issue

1

First Page

15

Last Page

20

ISSN

1874-2718

DOI

10.1007/s12104-018-9843-2

Keywords

Atrophin-1-interacting protein 4, E3 ubiquitin ligase, HECT, ITCH, NMR spectroscopy, Ubiquitin, Ubiquitylation

Cross Post Location

Student Publications

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Included in

Chemistry Commons

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