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 a-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.
Original language | Undefined/Unknown |
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Pages (from-to) | 535-545 |
Number of pages | 11 |
Journal | Trends in Biochemical Sciences |
Volume | 33 |
Issue number | 11 |
DOIs | |
Publication status | Published - 2008 |
Research programs
- EMC MGC-02-13-02