Belinda Camp
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Belinda Camp has a total of 9 co-authors. Here are the top co-authors by number of shared publications:
- Alberto Cristiani
Institute of Biochemistry II, Medical Faculty, Goethe University Frankfurt, Frankfurt am Main, Germany
1 shared publication - Aparna Viswanathan Ammanath
Institute of Biochemistry II, Medical Faculty, Goethe University Frankfurt, Frankfurt am Main, Germany
1 shared publication - Ivan Dikic
Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt, Germany
1 shared publication - Lina Herhaus
Helmholtz-Zentrum für Infektionsforschung
1 shared publication - Mahyar Aghapour
Department of Dermatology and Allergic Diseases, Ulm University, D-89081 Ulm, Germany
1 shared publication - Pauline Lascaux
Institute of Biochemistry II, Medical Faculty, Goethe University Frankfurt, Frankfurt am Main, Germany
1 shared publication
Latest Publications
- Open Access
- 13 May 2026
- Published by Springer Nature in Nature Communications
- Vol. 17 (1)
TBK1 restricts IRGQ-mediated autophagy
The autophagy-lysosome system directs the degradation of a wide variety of cytoplasmic cargo such as damaged organelles, protein aggregates, and invading pathogens. The autophagy receptor IRGQ harbors two distinct LIR domains, with LIR1 exhibiting high selectivity for GABARAPL2. Proteomic, biochemical, and high-throughput microscopy studies reveal that the IRGQ-GABARAPL2 complex functions as a hub for the interaction between hATG8s and the autophagy initiation machinery, promoting their lipidation and overall autophagic flux. The interaction of IRGQ with GABARAPL2 is regulated via TBK1. Upon TBK1 activation, GABARAPL2 is phosphorylated on S10, which disrupts IRGQ-GABARAPL2 complexation and therefore its interaction with the autophagy initiation machinery, resulting in a reduction of the autophagic flux of GABARAPL2 and IRGQ-cargo, without affecting bulk autophagy. These findings broaden IRGQ’s role in autophagy, identifying it as an interaction hub for autophagy initiation that is negatively regulated by TBK1.
- 13 May 2026
- Published by Springer Nature in Nature Communications
- Vol. 17 (1)
Open AccessTBK1 restricts IRGQ-mediated autophagy
The autophagy-lysosome system directs the degradation of a wide variety of cytoplasmic cargo such as damaged organelles, protein aggregates, and invading pathogens. The autophagy receptor IRGQ harbors two distinct LIR domains, with LIR1 exhibiting high selectivity for GABARAPL2. Proteomic, biochemical, and high-throughput microscopy studies reveal that the IRGQ-GABARAPL2 complex functions as a hub for the interaction between hATG8s and the autophagy initiation machinery, promoting their lipidation and overall autophagic flux. The interaction of IRGQ with GABARAPL2 is regulated via TBK1. Upon TBK1 activation, GABARAPL2 is phosphorylated on S10, which disrupts IRGQ-GABARAPL2 complexation and therefore its interaction with the autophagy initiation machinery, resulting in a reduction of the autophagic flux of GABARAPL2 and IRGQ-cargo, without affecting bulk autophagy. These findings broaden IRGQ’s role in autophagy, identifying it as an interaction hub for autophagy initiation that is negatively regulated by TBK1.