Discovery of new Longin and Roadblock domains that form platforms for small GTPases in Ragulator and TRAPP-II
| Autor: | Andreas Gerondopoulos, Louise H. Wong, Alberto T. Gatta, Tim P. Levine, Rachel D. Daniels, Francis A. Barr |
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Molecular Molecular Sequence Data Sequence alignment GTPase Biochemistry NPRL3 03 medical and health sciences 0302 clinical medicine NPRL2 C9orf72 Yeasts HBXIP Animals Guanine Nucleotide Exchange Factors Humans Amino Acid Sequence Letter to the Editor Peptide sequence Trs130p Monomeric GTP-Binding Proteins 030304 developmental biology Genetics 0303 health sciences biology YNR034W-A YCR075W-A Cell Biology Protein Structure Tertiary Highly sensitive TRAPP complex C7orf59 HHpred biology.protein DENNL72 Guanine nucleotide exchange factor 030217 neurology & neurosurgery |
| Zdroj: | Scopus-Elsevier Small GTPases |
| Popis: | Guanine nucleotide exchange factors (GEFs) control the site and extent of GTPase activity. Longin domains (LDs) are found in many Rab-GEFs, including DENNs, MON1/CCZ1, BLOC-3 and the TRAPP complex. Other GEFs, including Ragulator, contain roadblock domains (RDs), the structure of which is closely related to LDs. Other GTPase regulators, including mglB, SRX and Rags, use LDs or RDs as platforms for GTPases. Here, we review the conserved relationship between GTPases and LD/RDs, showing how LD/RD dimers act as adaptable platforms for GTPases. To extend our knowledge of GEFs, we used a highly sensitive sequence alignment tool to predict the existence of new LD/RDs. We discovered two yeast Ragulator subunits, and also a new LD in TRAPPC10 that may explain the Rab11-GEF activity ascribed to TRAPP-II. |
| Databáze: | OpenAIRE |
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