2026-06-14T03:35:59Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/57192024-09-27T10:16:53Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597
Repisalud
author
Plaza Menacho, Ivan
2018-03-09T11:13:28Z
2018-03-09T11:13:28Z
2018-02
Endocr Relat Cancer.2018; 25 (2): T79-T90.
10.1530/ERC-17-0354
1479-6821
1351-0088
Endocrine-related cancer
29175871
http://hdl.handle.net/20.500.12105/5719
It has been twenty-five years since the discovery of oncogenic germline RET mutations as the cause of multiple endocrine neoplasia type 2 (MEN2). Intensive work over the last two and a half decades on RET genetics, signaling and cell biology has provided the current bases for the genotype-phenotype and functional correlations within this cancer syndrome. On the contrary, the structural and molecular basis for RET tyrosine kinase domain activation and oncogenic deregulation has remained largely elusive. Recent studies with a strong crystallographic and biochemical focus have started to elucidate key insights into such molecular and atomic details revealing unexpected and private mechanisms of actions and molecular determinants not previously envisioned. This review focuses on the structure and function of the RET receptor, and in particular, on what a more detailed view of the protein itself and what the current structural and molecular information tell us about the genotype and phenotype relationships in the cancer syndrome MEN2.
eng
anti-cancer therapy
oncogene signaling
protein kinase
structure-function
Structure and function of RET in multiple endocrine neoplasia type 2
journal article
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structurefunctionRETmultiple_2018.pdf.txt