Proteomics

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HDX-MS of TRAPPII reveals a conserved Rab binding interface

ABSTRACT: We used hydrogen deuterium exchange mass spectrometry (HDX-MS) to define the interface of TRAPPII with three Rab GTPases (Rab1, Rab11, Rab43). These experiments were performed in the presence of EDTA to generate a nucleotide free stabilised Rab-GEF complex. Significant decreases in deuterium incorporation (defined as >4%, >0.4Da, two tailed T-test p value <0.01) were identified in the TRAPPC2L, TRAPPC4, and TRAPPC5 in the presence of Rab GTPases with no other changes in other TRAPP subunits. Here we show that all three Rab GTPases bind at a conserved interface of TRAPPII.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: John E Burke

PROVIDER: PXD020890 | Pride | 2020-12-11

REPOSITORIES: Pride

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Dataset's files

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Action DRS
02_8_19_KFHDX4_rab11_300s_3_0_01_11059.d.zip Other
02_8_19_KFHDX4_rab43_300s_3_0_01_11065.d.zip Other
06_8_19_2KFHDX4_apo_3000s_3_0_01_11069.d.zip Other
06_8_19_KFHDX4_apo_30s_3_0_01_11077.d.zip Other
06_8_19_KFHDX4_rab11_3000s_3_0_01_11073.d.zip Other
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Publications

The substrate specificity of the human TRAPPII complex's Rab-guanine nucleotide exchange factor activity.

Jenkins Meredith L ML   Harris Noah J NJ   Dalwadi Udit U   Fleming Kaelin D KD   Ziemianowicz Daniel S DS   Rafiei Atefeh A   Martin Emily M EM   Schriemer David C DC   Yip Calvin K CK   Burke John E JE  

Communications biology 20201204 1

The TRAnsport Protein Particle (TRAPP) complexes act as Guanine nucleotide exchange factors (GEFs) for Rab GTPases, which are master regulators of membrane trafficking in eukaryotic cells. In metazoans, there are two large multi-protein TRAPP complexes: TRAPPII and TRAPPIII, with the TRAPPII complex able to activate both Rab1 and Rab11. Here we present detailed biochemical characterisation of Rab-GEF specificity of the human TRAPPII complex, and molecular insight into Rab binding. GEF assays of  ...[more]

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