Grb2 is an adaptor protein thought to play an important role in ALK-mediated transformation, but its interaction with NPM-ALK, as well as its function in regulating ALCL signaling pathways and cell growth, has never been elucidated.

Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity. Large …

Nov 2, 2024 · Here, we use optogenetics and live-cell imaging to find that EML4-ALK assemblies suppress transmembrane receptor tyrosine kinase (RTK) signaling by sequestering RTK adapter proteins including...

Growth Factor Receptor-bound protein 2 (Grb2) is a key molecule in intracellular signal transduction, linking activated cell surface receptors to downstream targets by binding to specific phosphotyrosine-containing and proline-rich sequence motifs.

Feb 1, 2000 · Expression of full-length ATIC-ALK cDNA in mouse fibroblasts revealed that the fusion protein (a)possesses constitutive tyrosine kinase activity; (b)forms stable complexes with the signaling proteins Grb2 and Shc;(c) induces tyrosine-phosphorylation of Shc; and(d) provokes oncogenic transformation. These findings point to fusion with ATIC as an ...

Jul 11, 2019 · Unbiased CRISPR screens revealed a novel transcription hub containing IRF4 and BATF3, which directly control PD-L1 expression in ALK + ALCL. IRF4 and BATF3 are tightly regulated by a signaling network downstream of the nucleophosmin-ALK, through STAT3 and the GRB2/SOS1 signalosome.

Aug 20, 2010 · Grb2 is an adaptor protein thought to play an important role in ALK-mediated transformation, but its interaction with NPM-ALK, as well as its function in regulating ALCL signaling pathways and cell growth, has never been elucidated.

Aug 20, 2010 · Grb2 is an adaptor protein thought to play an important role in ALK-mediated transformation, but its interaction with NPM-ALK, as well as its function in regulating ALCL signaling pathways and...

We orthogonally confirmed recruitment of the key adaptor, GRB2, to endogenous EML4-ALK cytoplasmic protein granules detected by IF in patient-derived cancer cells (H3122) (Figure 2D), as well as through dual expression of EML4-ALK and GRB2 in Beas2B cells (Figure S2B).

We found EGFR bound to GRB2, suggesting how EGFR signaling can control this network and drive resistance to ALK TKI by facilitating EGFR-GRB2 signaling complexes. We found discoidin domain receptor tyrosine kinase 2 (DDR2), an RTK whose ligand is collagen, bound to both EML4-ALK and SHC1 baits.