Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Animals
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Conserved Sequence
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Cytoskeletal Proteins / chemistry
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism*
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Deubiquitinating Enzyme CYLD
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Dynactin Complex
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Humans
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Hypoparathyroidism / genetics
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Intellectual Disability / genetics
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Microtubule-Associated Proteins / genetics
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Microtubule-Associated Proteins / metabolism
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Microtubules / metabolism
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Models, Biological
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Models, Molecular
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Molecular Chaperones / genetics
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Molecular Sequence Data
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Muscular Atrophy, Spinal / genetics
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Mutation
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Neoplasm Proteins / metabolism
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Protein Structure, Tertiary
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Sequence Alignment
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Syndrome
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Tumor Suppressor Proteins / genetics
Substances
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Cytoskeletal Proteins
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Dynactin Complex
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Microtubule-Associated Proteins
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Molecular Chaperones
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Neoplasm Proteins
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TBCE protein, human
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Tumor Suppressor Proteins
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cytoplasmic linker protein 115
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cytoplasmic linker protein 170
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CYLD protein, human
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Deubiquitinating Enzyme CYLD