Preferred SH3 Domain Partners of ADAM Metalloproteases Include Shared and ADAM-Specific SH3 Interactions
| Autor: | Ari-Pekka J. Huovila, Iivari Kleino, Jussi Hepojoki, Annika Järviluoma, Kalle Saksela |
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| Přispěvatelé: | BioMediTech - BioMediTech, University of Tampere, Department of Virology, Medicum, Clinicum, Viral Zoonosis Research Unit |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Sorting Nexins
Protein domain PROMOTE MIGRATION lcsh:Medicine TYROSINE KINASE Computational biology Plasma protein binding macromolecular substances Biology SH3 domain Protein–protein interaction src Homology Domains SIGNALING PATHWAYS 03 medical and health sciences 0302 clinical medicine CYTOPLASMIC DOMAIN Lääketieteen bioteknologia - Medical biotechnology Disintegrin Humans BREAST-CANCER lcsh:Science 030304 developmental biology Genetics 0303 health sciences Multidisciplinary lcsh:R Signal transducing adaptor protein ECTODOMAIN CLEAVAGE ADAM Proteins carbohydrates (lipids) HEK293 Cells ALTERNATIVE EXON USE TEC FAMILY KINASES 030220 oncology & carcinogenesis biology.protein lcsh:Q TRANSFORMED-CELLS 3111 Biomedicine Carrier Proteins GROWTH-FACTOR RECEPTOR Protein Binding Research Article |
| Zdroj: | PLoS ONE PLoS ONE, Vol 10, Iss 3, p e0121301 (2015) |
| Popis: | A disintegrin and metalloproteinases (ADAMs) constitute a protein family essential for extracellular signaling and regulation of cell adhesion. Catalytic activity of ADAMs and their predicted potential for Src-homology 3 (SH3) domain binding show a strong correlation. Here we present a comprehensive characterization of SH3 binding capacity and preferences of the catalytically active ADAMs 8, 9, 10, 12, 15, 17, and 19. Our results revealed several novel interactions, and also confirmed many previously reported ones. Many of the identified SH3 interaction partners were shared by several ADAMs, whereas some were ADAM-specific. Most of the ADAM-interacting SH3 proteins were adapter proteins or kinases, typically associated with sorting and endocytosis. Novel SH3 interactions revealed in this study include TOCA1 and CIP4 as preferred partners of ADAM8, and RIMBP1 as a partner of ADAM19. Our results suggest that common as well as distinct mechanisms are involved in regulation and execution of ADAM signaling, and provide a useful framework for addressing the pathways that connect ADAMs to normal and aberrant cell behavior. Public Library of Science open access |
| Databáze: | OpenAIRE |
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