Interactome Profiling of a Lysine Deacetylase Trapping Probe Library Uncovers Crosstalk Between HDAC6 and NF‐κB Signaling

J Julian Seidel (Interfaculty Institute of Biochemistry, University of Tübingen) C Caroline Schönfeld (Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany) J Julia Sindlinger (Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany) J Jürgen Eirich (Plant Physiology, Institute of Plant Biology and Biotechnology, University of Münster) S Sören Kirchgäßner (Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany) N Nina Kreienkamp (Department of Medicine A, Hematology, Oncology, and Pneumology University Hospital Münster Albert‐Schweitzer‐Campus 1 48149 Münster Germany) K Klaus Schulze‐Osthoff (Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany) I Iris Finkemeier (Plant Physiology, Institute of Plant Biology and Biotechnology, University of Münster) S Stephan Hailfinger (Department of Medicine A, Hematology, Oncology, and Pneumology University Hospital Münster Albert‐Schweitzer‐Campus 1 48149 Münster Germany) D Dirk Schwarzer (Interfaculty Institute of Biochemistry, University of Tübingen)

Abstract

AbstractLysine or histone deacetylases (HDACs) remove acetyl groups from lysine residues of numerous proteins, thereby regulating their function and activity. HDAC6 is involved in multiple cellular processes, yet its protein interaction network remains poorly understood. To uncover novel HDAC6 substrates, we performed an acetylome analysis of HDAC6 knockdown cells, which served as a basis for the design of an HDAC6‐trapping peptide library containing hydroxamic acids. Most probes enriched HDAC6 from cell lysates stronger than HDAC1. Proteomic profiling of the trapping probes revealed a preferential enrichment of HDAC6 and resulted in the identification of novel putative HDAC6 interaction partners. Among those were several components of the pro‐inflammatory transcription factor NF‐κB that were independently confirmed as HDAC6 binders. Mechanistically, HDAC6 counteracted NF‐κB activity induced upon p300‐catalyzed acetylation of NF‐κB p50. These findings indicate a potential anti‐inflammatory function of HDAC6 in NF‐κB signaling.

Article Details

Volume / Issue Vol. 64, Issue 40
Published September 26, 2025
ISSN 1433-7851
Publisher Wiley

Journal Info

Angewandte Chemie International Edition

Wiley

ISSN: 1433-7851 Physical Sciences

Authors (10)

J

Julian Seidel

Interfaculty Institute of Biochemistry, University of Tübingen

C

Caroline Schönfeld

Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany

J

Julia Sindlinger

Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany

J

Jürgen Eirich

Plant Physiology, Institute of Plant Biology and Biotechnology, University of Münster

S

Sören Kirchgäßner

Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany

N

Nina Kreienkamp

Department of Medicine A, Hematology, Oncology, and Pneumology University Hospital Münster Albert‐Schweitzer‐Campus 1 48149 Münster Germany

K

Klaus Schulze‐Osthoff

Interfaculty Institute of Biochemistry (IFIB) University of Tübingen Auf der Morgenstelle 34 72076 Tübingen Germany

I

Iris Finkemeier

Plant Physiology, Institute of Plant Biology and Biotechnology, University of Münster

S

Stephan Hailfinger

Department of Medicine A, Hematology, Oncology, and Pneumology University Hospital Münster Albert‐Schweitzer‐Campus 1 48149 Münster Germany

D

Dirk Schwarzer

Interfaculty Institute of Biochemistry, University of Tübingen