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TitleStructural insights into WHAMM-mediated cytoskeletal coordination during membrane remodeling.
Journal, issue, pagesJ Cell Biol, Vol. 199, Issue 1, Page 111-124, Year 2012
Publish dateOct 1, 2012
AuthorsQing-Tao Shen / Peter P Hsiue / Charles V Sindelar / Matthew D Welch / Kenneth G Campellone / Hong-Wei Wang /
PubMed AbstractThe microtubule (MT) and actin cytoskeletons drive many essential cellular processes, yet fairly little is known about how their functions are coordinated. One factor that mediates important cross ...The microtubule (MT) and actin cytoskeletons drive many essential cellular processes, yet fairly little is known about how their functions are coordinated. One factor that mediates important cross talk between these two systems is WHAMM, a Golgi-associated protein that utilizes MT binding and actin nucleation activities to promote membrane tubulation during intracellular transport. Using cryoelectron microscopy and other biophysical and biochemical approaches, we unveil the underlying mechanisms for how these activities are coordinated. We find that WHAMM bound to the outer surface of MT protofilaments via a novel interaction between its central coiled-coil region and tubulin heterodimers. Upon the assembly of WHAMM onto MTs, its N-terminal membrane-binding domain was exposed at the MT periphery, where it can recruit vesicles and remodel them into tubular structures. In contrast, MT binding masked the C-terminal portion of WHAMM and prevented it from promoting actin nucleation. These results give rise to a model whereby distinct MT-bound and actin-nucleating populations of WHAMM collaborate during membrane tubulation.
External linksJ Cell Biol / PubMed:23027905 / PubMed Central
MethodsEM (helical sym.)
Resolution18.0 - 22.0 Å
Structure data

EMDB-2157:
Helical structures of WHAMM around MTs revealed by Electron cryo-microscopy
Method: EM (helical sym.) / Resolution: 18.0 Å

EMDB-5463:
Electron cryo-microscopy of WHAMM coiled-coil domain and MTs
Method: EM (helical sym.) / Resolution: 22.0 Å

Source
  • Homo sapiens (human)

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