Proteomics

Dataset Information

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Detailing the Structural and Dynamic Interactions Between WDR44 and Rab11

ABSTRACT: DR44 is a Rab11 effector protein that is thought to regulate ciliogenesis by competing with pro-ciliogenesis factors for Rab11 binding. The structure of WDR44 and the molecular mechanism of its interaction with Rab11 is unknown. To explore the interactions between these two proteins multiple WDR44 constructs were designed and pulled down with Rab11. Using the results of the pulldown assay as a guide we used protein complex prediction software, and hydrogen deuterium exchange mass spectrometry (HDX-MS) to identify the binding interface between WDR44 and Rab11. Mutagenesis was used to make specific mutations in the putative Rab11 binding region of WDR44.

INSTRUMENT(S): impact HD

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: John Burke  

LAB HEAD: Dr. John E. Burke

PROVIDER: PXD035741 | Pride | 2023-03-11

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
02_07_22_NHHDX7_PA_0.3s_1_0_01_18776.d.zip Other
02_07_22_NHHDX7_PA_ND_0_01_18770.d.zip Other
02_07_22_NHHDX7_PC_0.3s_1_0_01_18780.d.zip Other
02_07_22_NHHDX7_R_ND_0_01_18774.d.zip Other
02_07_22_NHHDX7_UA_0.3s_1_0_01_18778.d.zip Other
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Publications

Molecular basis for the recruitment of the Rab effector protein WDR44 by the GTPase Rab11.

Thibodeau Matthew C MC   Harris Noah J NJ   Jenkins Meredith L ML   Parson Matthew A H MAH   Evans John T JT   Scott Mackenzie K MK   Shaw Alexandria L AL   Pokorný Daniel D   Leonard Thomas A TA   Burke John E JE  

The Journal of biological chemistry 20221201 1

The formation of complexes between Rab11 and its effectors regulates multiple aspects of membrane trafficking, including recycling and ciliogenesis. WD repeat-containing protein 44 (WDR44) is a structurally uncharacterized Rab11 effector that regulates ciliogenesis by competing with prociliogenesis factors for Rab11 binding. Here, we present a detailed biochemical and biophysical characterization of the WDR44-Rab11 complex and define specific residues mediating binding. Using AlphaFold2 modeling  ...[more]

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