Volume 32, No 2, Feb 2022

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 32 Issue 2, February 2022: 117-118

RESEARCH HIGHLIGHTS

SPFH protein cage — one ring to rule them all

Oliver Daumke^1,2,* , Gary R. Lewin³

¹Crystallography, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany
²Institute of Chemistry and Biochemistry, Freie Universität Berlin, Berlin, Germany
³Molecular Physiology of Somatic Sensation, Department of Neuroscience, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin, Germany
Correspondence: Oliver Daumke(oliver.daumke@mdc-berlin.de)

Stomatin/prohibitin/flotillin/HflKC (SPFH) proteins comprise a universally conserved family of membrane-associated scaffolds that compartmentalize membranes, but the detailed molecular mechanism has remained unclear. In a recent paper published in Cell Research, Ma et al. determined the cryo-EM structure of the bacterial SPFH heterodimer HflK/C, which assembles into a giant molecular cage encasing four AAA+ protease hexamers; the structural work elucidates how SPFH proteins confine their client proteins in specialized membrane microdomains.

https://doi.org/10.1038/s41422-021-00605-7

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