Mechanism and evolution of the Zn-fingernail required for interaction of VARP with VPS29

Autor: Harriet Crawley-Snowdon, Ji-Chun Yang, Nathan R. Zaccai, Luther J. Davis, Lena Wartosch, Emily K. Herman, Nicholas A. Bright, James S. Swarbrick, Brett M. Collins, Lauren P. Jackson, Matthew N. J. Seaman, J. Paul Luzio, Joel B. Dacks, David Neuhaus, David J. Owen
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Zdroj: Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Druh dokumentu: article
ISSN: 2041-1723
DOI: 10.1038/s41467-020-18773-2
Popis: VARP is bound to endosomes and functions as a protein:protein interaction platform. Here, the authors present the NMR structure of the complex between the retromer subunit VPS29 and a VARP Zn-fingernail microdomain that is structurally distinct from Zn-fingers and further show that mutations, which abolish VPS29:VARP binding, inhibit trafficking from endosomes to the cell surface.
Databáze: Directory of Open Access Journals