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The anaplastic lymphoma kinase (ALK) was first discovered in 1994 as a tyrosine kinase in a type of lymphoma cancer cell. The specific type of tyrosine kinase ALK is classified as is a [https://link.springer.com/article/10.1186/s12943-018-0782-4 receptor tyrosine kinase] (RTK) and like other RTKs, it's an integral protein with extracellular and intracellular domains and is involved in transmembrane signaling and communication within the cell. ALK is commonly expressed in the development of the nervous system. Anaplastic lymphoma kinase receptor (ALKr) is the extracellular portion of the [https://pubmed.ncbi.nlm.nih.gov/32114309/ RTK] that includes a binding surface for a ligand to bind. When the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5789956/ ALK activating ligand] (ALKAL) binds to ALKr, this causes a conformational change of ALK, allowing the intracellular kinase domain of ALK to phosphorylate [https://www.ncbi.nlm.nih.gov/books/NBK553175/ a] tyrosine residue on a downstream enzyme, which will activate this enzyme and activate a signaling cascade. Abnormal forms of ALK are closely related to the formation of several cancers. <ref>DOI: 10.3390/ijms19113448</ref>