Article abstract
Nature Structural & Molecular Biology 14, 959 - 967 (2007)
Published online: 9 September 2007 | doi:10.1038/nsmb1291
Structure-function relationship of CAP-Gly domains
Anke Weisbrich1,4, Srinivas Honnappa1,4, Rolf Jaussi1, Oksana Okhrimenko2, Daniel Frey1, Ilian Jelesarov2, Anna Akhmanova3 & Michel O Steinmetz1
Abstract
In all eukaryotes, CAP-Gly proteins control important cellular processes. The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed between the CAP-Gly domain of p150glued and the C-terminal zinc knuckle of CLIP170 as a model system to explore the structure-function relationship of CAP-Gly–mediated protein interactions. We demonstrate that the conserved GKNDG motif of CAP-Gly domains is responsible for targeting to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and microtubules. The CAP-Gly–EEY/F interaction is essential for the recruitment of the dynactin complex by CLIP170 and for activation of CLIP170. Our findings define the molecular basis of CAP-Gly domain function, including the tubulin detyrosination-tyrosination cycle. They further establish fundamental roles for the interaction between CAP-Gly proteins and C-terminal EEY/F sequence motifs in regulating complex and dynamic cellular processes.
- Biomolecular Research, Structural Biology, Paul Scherrer Insititut, CH-5232 Villigen PSI, Switzerland.
- Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland.
- Department of Cell Biology, Erasmus Medical Center, P.O. Box 2040, 3000 CA Rotterdam, The Netherlands.
- These authors contributed equally to this work.
Correspondence to: Michel O Steinmetz1 e-mail: michel.steinmetz@psi.ch
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