VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.

Autor:	Zhang J; Department of Biochemistry and Molecular Biology, The Uniformed Services University of the Health Sciences - F. Edward Hébert School of Medicine, Bethesda, MD 20814, USA., Qiu R; Department of Biochemistry and Molecular Biology, The Uniformed Services University of the Health Sciences - F. Edward Hébert School of Medicine, Bethesda, MD 20814, USA., Xie S; Department of Biochemistry and Molecular Biology, The Uniformed Services University of the Health Sciences - F. Edward Hébert School of Medicine, Bethesda, MD 20814, USA; Montgomery Blair High School, Silver Spring, MD, USA., Rasmussen M; Department of Biochemistry and Molecular Biology, The Uniformed Services University of the Health Sciences - F. Edward Hébert School of Medicine, Bethesda, MD 20814, USA., Xiang X; Department of Biochemistry and Molecular Biology, The Uniformed Services University of the Health Sciences - F. Edward Hébert School of Medicine, Bethesda, MD 20814, USA. Electronic address: xin.xiang@usuhs.edu.
Jazyk:	angličtina
Zdroj:	Cell reports [Cell Rep] 2024 Nov 26; Vol. 43 (11), pp. 114943. Date of Electronic Publication: 2024 Nov 01.
DOI:	10.1016/j.celrep.2024.114943
Abstrakt:	Cytoplasmic dynein-mediated intracellular transport needs the multi-component dynactin complex for cargo binding and motor activation. However, the cellular factors involved in dynactin assembly remain unexplored. Here, we found in Aspergillus nidulans that the vezatin homolog VezA is important for dynactin assembly. VezA affects the microtubule plus-end accumulation of dynein before cargo binding and cargo-adapter-mediated dynein activation, two processes that both need dynactin. The dynactin complex contains multiple components, including p150, p50, and an Arp1 (actin-related protein 1) mini-filament associated with a pointed-end sub-complex. VezA physically interacts with the Arp1 mini-filament either directly or indirectly. Loss of VezA significantly decreases the amount of Arp1 pulled down with pointed-end proteins, as well as the protein levels of p50 and p150 in cell extract. Using various dynactin mutants, we further revealed that the dynactin assembly process must be highly coordinated. Together, these results shed light on dynactin assembly in vivo. Competing Interests: Declaration of interests The authors declare no competing interest. (Published by Elsevier Inc.)
Databáze:	MEDLINE
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