9BQX

Membrane-bound AMPH-1 tube in the presence of GTP

This is a non-PDB format compatible entry.

Summary for 9BQX

• Entry DOI: 10.2210/pdb9bqx/pdb
• EMDB information: 44828
• Descriptor: Amphiphysin (1 entity in total)
• Functional Keywords: membrane tubulation protein complex, lipid binding protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 4
• Total formula weight: 109720.20

Authors

Wang, Y.,Gai, W.,Zhang, J.,Rye, H. (deposition date: 2024-05-10, release date: 2025-05-14)

Primary citation

Kustigian, L.,Gong, X.,Gai, W.,Thongchol, J.,Zhang, J.,Puchalla, J.,Carr, C.M.,Rye, H.S.
GTP-stimulated membrane fission by the N-BAR protein AMPH-1.
Traffic, 24:34-47, 2023

PubMed Abstract: Membrane-enclosed transport carriers sort biological molecules between stations in the cell in a dynamic process that is fundamental to the physiology of eukaryotic organisms. While much is known about the formation and release of carriers from specific intracellular membranes, the mechanism of carrier formation from the recycling endosome, a compartment central to cellular signaling, remains to be resolved. In Caenorhabditis elegans, formation of transport carriers from the recycling endosome requires the dynamin-like, Eps15-homology domain (EHD) protein, RME-1, functioning with the Bin/Amphiphysin/Rvs (N-BAR) domain protein, AMPH-1. Here we show, using a free-solution single-particle technique known as burst analysis spectroscopy (BAS), that AMPH-1 alone creates small, tubular-vesicular products from large, unilamellar vesicles by membrane fission. Membrane fission requires the amphipathic H0 helix of AMPH-1 and is slowed in the presence of RME-1. Unexpectedly, AMPH-1-induced membrane fission is stimulated in the presence of GTP. Furthermore, the GTP-stimulated membrane fission activity seen for AMPH-1 is recapitulated by the heterodimeric N-BAR amphiphysin protein from yeast, Rvs161/167p, strongly suggesting that GTP-stimulated membrane fission is a general property of this important class of N-BAR proteins.

PubMed: 36435193
DOI: 10.1111/tra.12875

Experimental method

ELECTRON MICROSCOPY (7.9 Å)