5X1G

WHAMM's Microtubule binding motif

Summary for 5X1G

• Entry DOI: 10.2210/pdb5x1g/pdb
• EMDB information: 6701
• Descriptor: WASP homolog-associated protein with actin, membranes and microtubules (1 entity in total)
• Functional Keywords: microtubule, helical reconstruction, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 4414.18

Authors

Liu, T.,Wang, H.W. (deposition date: 2017-01-25, release date: 2017-07-05, Last modification date: 2024-03-27)

Primary citation

Liu, T.,Dai, A.,Cao, Y.,Zhang, R.,Dong, M.Q.,Wang, H.W.
Structural Insights of WHAMM's Interaction with Microtubules by Cryo-EM
J. Mol. Biol., 429:1352-1363, 2017

PubMed Abstract: WASP homolog associated with actin, membranes, and microtubules (WHAMM) is a vertebrate protein functioning in membrane tubulation for intracellular membrane trafficking and specific organelle formation. Composed of multiple domains, WHAMM can bind to membrane and microtubule (MT) and promote actin polymerization nucleation. Previous work revealed that WHAMM's activity to promote actin nucleation is repressed upon binding to MTs. Here, we discovered that WHAMM interacts with αβ-tubulin through a small peptide motif within its MT-binding domain. We reconstructed a high-resolution structure of WHAMM's MT-binding motif (MBM) assembling around MTs using cryo-electron microscopy and verified it with chemical cross-linking and mass spectrometry analysis. We also detected a conformational switch of this motif between the non-MT-bound state and the MT-bound state. These discoveries provide new insights into the mechanism by which WHAMM coordinates actin and MT networks, the two major cytoskeletal systems involved in membrane trafficking and membrane remodeling.

PubMed: 28351611
DOI: 10.1016/j.jmb.2017.03.022

Experimental method

ELECTRON MICROSCOPY (4.5 Å)