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Identification of APBB1 as a substrate for anaplastic lymphoma kinase.
Suzuki, Yuji; Tsubota, Shoma; Kadomatsu, Kenji; Sakamoto, Kazuma.
Afiliación
  • Suzuki Y; Department of Integrative Physiology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya, Aichi 466-8550, Japan.
  • Tsubota S; Department of Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya, Aichi 466-8550, Japan.
  • Kadomatsu K; Department of Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku, Nagoya, Aichi 466-8550, Japan.
  • Sakamoto K; Institute for Glyco-core Research, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601, Japan.
J Biochem ; 176(5): 395-403, 2024 Nov 04.
Article en En | MEDLINE | ID: mdl-39115278
ABSTRACT
Anaplastic lymphoma kinase (ALK) is a well-known oncogene involved in various malignancies such as anaplastic large cell lymphoma, lung cancer and neuroblastoma. Several substrates for fused ALK have been identified and their biological functions have been described. However, the lack of a comprehensive identification of ALK substrates limits our understanding of the biological roles of receptor ALK. Thus, this study aimed to identify novel ALK substrates and characterize their biological functions. We screened the interactors of the kinase domain of receptor ALK using proximity-dependent biotin identification and identified 43 interactors. We narrowed down the candidates by evaluating whether these interactors were downstream of ALK in a neuroblastoma cell line, NB-1. Amongst these, we identified amyloid beta precursor protein-binding family B member 1 (APBB1) as an ALK downstream molecule involved in NB-1 cell viability. Finally, we assessed the kinase-substrate relationship between ALK and APBB1 and found that ALK phosphorylated multiple tyrosine residues in APBB1 both in-cell and in-tube assays, with tyrosine 269 as a major target. In conclusion, we successfully identified a new substrate for receptor ALK. Our results may help further elucidate the molecular mechanism of ALK downstream signalling in neuroblastoma.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Quinasa de Linfoma Anaplásico Límite: Humans Idioma: En Revista: J Biochem Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Quinasa de Linfoma Anaplásico Límite: Humans Idioma: En Revista: J Biochem Año: 2024 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido