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Trends Biochem Sci. 2008 Nov;33(11):535-45. doi: 10.1016/j.tibs.2008.08.006. Epub 2008 Oct 4.

Capturing protein tails by CAP-Gly domains.

Author information

1
Biomolecular Research, Structural Biology, Paul Scherrer Insititut, Villigen PSI, Switzerland. michel.steinmetz@psi.ch

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.

PMID:
18835717
DOI:
10.1016/j.tibs.2008.08.006
[Indexed for MEDLINE]

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