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WW domains provide a platform for the assembly of multiprotein networks

Ingham, R. J. and Colwill, K. and Howard, C. and Dettwiler, S. and Lim, C. S. H. and Yu, J. and Hersi, K. and Raaijmakers, J. and Gish, G. and Mbamalu, G. and Taylor, L. and Yeung, B. and Vassilovski, G. and Amin, M. and Chen, F. and Matskova, L. and Winberg, G. and Ernberg, I. and Linding, R. and O'Donnell, P. and Starostine, A. and Keller, W. and Metalnikov, P. and Stark, C. and Pawson, T.. (2005) WW domains provide a platform for the assembly of multiprotein networks. Molecular and Cellular Biology, 25 (16). pp. 7092-7106.

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Abstract

WW domains are protein modules that mediate protein-protein interactions through recognition of proline-rich peptide motifs and phosphorylated serine/threonine-proline sites. To pursue the functional properties of WW domains, we employed mass spectrometry to identify 148 proteins that associate with 10 human WW domains. Many of these proteins represent novel WW domain-binding partners and are components of multiprotein complexes involved in molecular processes, such as transcription, RNA processing, and cytoskeletal regulation. We validated one complex in detail, showing that WW domains of the AIP4 E3 protein-ubiquitin ligase bind directly to a PPXY motif in the p68 subunit of pre-mRNA cleavage and polyadenylation factor Im in a manner that promotes p68 ubiquitylation. The tested WW domains fall into three broad groups on the basis of hierarchical clustering with respect to their associated proteins; each such cluster of bound proteins displayed a distinct set of WW domain-binding motifs. We also found that separate WW domains from the same protein or closely related proteins can have different specificities for protein ligands and also demonstrated that a single polypeptide can bind multiple classes of WW domains through separate proline-rich motifs. These data suggest that WW domains provide a versatile platform to link individual proteins into physiologically important networks.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Keller)
05 Faculty of Science > Departement Biozentrum > Growth & Development
UniBasel Contributors:Keller, Walter
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:American Society for Microbiology
ISSN:0270-7306
e-ISSN:1098-5549
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:08 Nov 2017 10:13
Deposited On:22 Mar 2012 13:19

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