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Capturing protein tails by CAP-Gly domains.
Journal article

Capturing protein tails by CAP-Gly domains.

  • Steinmetz MO Biomolecular Research, Structural Biology, Paul Scherrer Insititut, Villigen PSI, Switzerland. michel.steinmetz@psi.ch
  • Akhmanova A
  • 2008-10-07
Published in:
  • 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
English 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.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.ch/global/documents/68808
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