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TitleBiochemical Insight into Novel Rab-GEF Activity of the Mammalian TRAPPIII Complex.
Journal, issue, pagesJ Mol Biol, Vol. 433, Issue 18, Page 167145, Year 2021
Publish dateSep 3, 2021
AuthorsNoah J Harris / Meredith L Jenkins / Udit Dalwadi / Kaelin D Fleming / Sung-Eun Nam / Matthew A H Parson / Calvin K Yip / John E Burke /
PubMed AbstractTransport Protein Particle complexes (TRAPP) are evolutionarily conserved regulators of membrane trafficking, with this mediated by their guanine nucleotide exchange factor (GEF) activity towards Rab ...Transport Protein Particle complexes (TRAPP) are evolutionarily conserved regulators of membrane trafficking, with this mediated by their guanine nucleotide exchange factor (GEF) activity towards Rab GTPases. In metazoans evidence suggests that two different TRAPP complexes exist, TRAPPII and TRAPPIII. These two complexes share a common core of subunits, with complex specific subunits (TRAPPC9 and TRAPPC10 in TRAPPII and TRAPPC8, TRAPPC11, TRAPPC12, TRAPPC13 in TRAPPIII). TRAPPII and TRAPPIII have distinct specificity for GEF activity towards Rabs, with TRAPPIII acting on Rab1, and TRAPPII acting on Rab1 and Rab11. The molecular basis for how these complex specific subunits alter GEF activity towards Rab GTPases is unknown. Here we have used a combination of biochemical assays, hydrogen deuterium exchange mass spectrometry (HDX-MS) and electron microscopy to examine the regulation of TRAPPII and TRAPPIIII complexes in solution and on membranes. GEF assays revealed that TRAPPIII has GEF activity against Rab1 and Rab43, with no detectable activity against the other 18 Rabs tested. The TRAPPIII complex had significant differences in protein dynamics at the Rab binding site compared to TRAPPII, potentially indicating an important role of accessory subunits in altering the active site of TRAPP complexes. Both the TRAPPII and TRAPPIII complexes had enhanced GEF activity on lipid membranes, with HDX-MS revealing numerous conformational changes that accompany membrane association. HDX-MS also identified a membrane binding site in TRAPPC8. Collectively, our results provide insight into the functions of TRAPP complexes and how they can achieve Rab specificity.
External linksJ Mol Biol / PubMed:34229011
MethodsEM (single particle)
Resolution14.2 Å
Structure data

EMDB-23997:
Structure of the mammalian Transport Protein Particle Complex (TRAPP) III
Method: EM (single particle) / Resolution: 14.2 Å

Source
  • Homo sapiens (human)

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