biostudies-literaturePinet LUniversity of Paris-SudAgence Nationale de la Recherche1690https://www.ebi.ac.uk/biostudies/studies/S-EPMC8615588biostudies-literatureUnknown11(11)ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally. However, their whole C-terminal tails (CTs) following the kinase domain were only described at atomic resolution in the last 4 years. They were shown to be intrinsically disordered. The CTs are known to be tyrosine-phosphorylated when the activated homo- or hetero-dimers of ErbBs are formed. Their phosphorylation triggers interaction with phosphotyrosine binding (PTB) or Src Homology 2 (SH2) domains and activates several signaling pathways controling cellular motility, proliferation, adhesion, and apoptosBiomoleculesExpanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.PMC8615588ANR-13-BSV8-00162019SACLS375Assrir Nvan Heijenoort CPinet LfalseExpanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally. However, their whole C-terminal tails (CTs) following the kinase domain were only described at atomic resolution in the last 4 years. They were shown to be intrinsically disordered. The CTs are known to be tyrosine-phosphorylated when the activated homo- or hetero-dimers of ErbBs are formed. Their phosphorylation triggers interaction with phosphotyrosine binding (PTB) or Src Homology 2 (SH2) domains and activates several signaling pathways controling cellular motility, proliferation, adhesion, and apoptos2021-01-01T00:00:00Z2021 Nov2025-04-04T21:10:59.179Z2022-02-11T13:22:45.203ZS-EPMC86155883482768810.3390/biom11111690