% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{MonteroVergara:286713,
author = {J. Montero-Vergara and K. Plachetta and L. Kinch and S.
Bernhardt$^*$ and K. Kashyap and B. Levine and L. Thukral
and M. Vetter and C. Thomssen and S. Wiemann$^*$ and S.
Peña-Llopis$^*$ and V. Jendrossek and S.
Vega-Rubin-de-Celis},
title = {{GRB}2 is a {BECN}1 interacting protein that regulates
autophagy.},
journal = {Cell death $\&$ disease},
volume = {15},
number = {1},
issn = {2041-4889},
address = {London [u.a.]},
publisher = {Nature Publishing Group},
reportid = {DKFZ-2024-00053},
pages = {14},
year = {2024},
abstract = {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.},
cin = {B050 / ED01},
ddc = {570},
cid = {I:(DE-He78)B050-20160331 / I:(DE-He78)ED01-20160331},
pnm = {312 - Funktionelle und strukturelle Genomforschung
(POF4-312)},
pid = {G:(DE-HGF)POF4-312},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:38182563},
pmc = {pmc:PMC10770341},
doi = {10.1038/s41419-023-06387-7},
url = {https://inrepo02.dkfz.de/record/286713},
}