Steinmetz MO Akhmanova A 2008 Cytoskeleton-associated protein-glycine-rich (CAP-Gly) domains are protein-interaction modules implicated in important cellular processes and in hereditary human diseases. A prominent function of CAP-Gly domains is to bind to C-terminal EEY/F-COO(-) sequence motifs present in alpha-tubulin and in some microtubule-associated protein tails; however, CAP-Gly domains also interact with other structural elements including end-binding homology domains, zinc-finger motifs and proline-rich sequences. Recent findings unravelled the link between tubulin tyrosination and CAP-Gly-protein recruitment to microtubules. They further provided a molecular basis for understanding the role of CAP-Gly domains in controlling dynamic cellular processes including the tracking and regulation of microtubule ends. It is becoming increasingly clear that CAP-Gly domains are also involved in coordinating complex and diverse aspects of cell architecture and signalling. https://sonar.ch/global/documents/68808 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.tibs.2008.08.006 info:eu-repo/semantics/altIdentifier/pmid/18835717 Trends in biochemical sciences. - 2008 Amino Acid Sequence Animals Conserved Sequence Cytoskeletal Proteins Deubiquitinating Enzyme CYLD Dynactin Complex Humans Hypoparathyroidism Intellectual Disability Microtubule-Associated Proteins Microtubules Models, Biological Models, Molecular Molecular Chaperones Molecular Sequence Data Muscular Atrophy, Spinal Mutation Neoplasm Proteins Protein Structure, Tertiary Sequence Alignment Syndrome Tumor Suppressor Proteins Capturing protein tails by CAP-Gly domains. http://purl.org/coar/resource_type/c_6501