6KU0

Crystal structure of MyoVa-GTD in complex with MICAL1-GTBM

Summary for 6KU0

• Entry DOI: 10.2210/pdb6ku0/pdb
• Descriptor: Unconventional myosin-Va, Peptide from [F-actin]-monooxygenase MICAL1, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: complex, cargo binding, protein binding
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 95200.06

Authors

Niu, F.,Wei, Z. (deposition date: 2019-08-29, release date: 2020-09-02, Last modification date: 2023-11-22)

Primary citation

Niu, F.,Sun, K.,Wei, W.,Yu, C.,Wei, Z.
F-actin disassembly factor MICAL1 binding to Myosin Va mediates cargo unloading during cytokinesis.
Sci Adv, 6:-, 2020

PubMed Abstract: Motor-mediated intracellular trafficking requires motors to position cargoes at proper locations. Myosin Va (MyoVa), an actin-based motor, is a classic model for studying cargo transport. However, the molecular basis underlying cargo unloading in MyoVa-mediated transport has remained enigmatic. We have identified MICAL1, an F-actin disassembly regulator, as a binding partner of MyoVa and shown that MICAL1-MyoVa interaction is critical for localization of MyoVa at the midbody. By binding to MICAL1, MyoVa-mediated transport is terminated, resulting in vesicle unloading at the midbody for efficient cytokinesis. The MyoVa/MICAL1 complex structure reveals that MICAL1 and F-actin assembly factors, Spires, share an overlapped binding surface on MyoVa, suggesting a regulatory role of F-actin dynamics in cargo unloading. Down-regulating F-actin disassembly by a MICAL1 mutant significantly reduces MyoVa and vesicles accumulating at the midbody. Collectively, our findings demonstrate that MyoVa binds to MICAL1 at the midbody destination and triggers F-actin disassembly to unload the vesicle cargo.

PubMed: 33158857
DOI: 10.1126/sciadv.abb1307

Experimental method

X-RAY DIFFRACTION (1.6 Å)