GRB2 is a BECN1 interacting protein that regulates autophagy

GRB2 is an adaptor protein of HER2 (and several other tyrosine kinases), which we identified as a novel BECN1 (Beclin 1) interacting partner. GRB2 co-immunoprecipitated with BECN1 in several breast cancer cell lines and regulates autophagy through a mechanism involving the modulation of the class II...

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Bibliographic Details
Published in:Cell death & disease 2024-01, Vol.15 (1), p.14-14, Article 14
Main Authors: Montero-Vergara, Jetsy, Plachetta, Kira, Kinch, Lisa, Bernhardt, Stephan, Kashyap, Kriti, Levine, Beth, Thukral, Lipi, Vetter, Martina, Thomssen, Christoph, Wiemann, Stefan, Peña-Llopis, Samuel, Jendrossek, Verena, Vega-Rubin-de-Celis, Silvia
Format: Article
Language:English
Subjects:
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Adapter proteins
Adaptor Proteins, Signal Transducing
Animals
Antibodies
Autophagy
Beclin-1 - metabolism
Biochemistry
Biomedical and Life Sciences
Breast cancer
Cancer research
Carcinogenesis
Cell Biology
Cell Culture
Cell death
Cell Transformation, Neoplastic
Chorioallantoic membrane
ErbB-2 protein
Genomics
GRB2 Adaptor Protein - metabolism
Grb2 protein
Humans
Immunology
Kinases
Life Sciences
Medical research
Phosphorylation
Tumor cell lines
Tumorigenesis
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Summary:GRB2 is an adaptor protein of HER2 (and several other tyrosine kinases), which we identified as a novel BECN1 (Beclin 1) interacting partner. GRB2 co-immunoprecipitated with BECN1 in several breast cancer cell lines and regulates autophagy through a mechanism involving the modulation of the class III PI3Kinase VPS34 activity. In ovo studies in a CAM (Chicken Chorioallantoic Membrane) model indicated that GRB2 knockdown, as well as overexpression of GRB2 loss-of-function mutants (Y52A and S86A-R88A) compromised tumor growth. These differences in tumor growth correlated with differential autophagy activity, indicating that autophagy effects might be related to the effects on tumorigenesis. Our data highlight a novel function of GRB2 as a BECN1 binding protein and a regulator of autophagy.
ISSN:2041-4889
2041-4889
DOI:10.1038/s41419-023-06387-7