6UP6

Endophilin B1 helical scaffold

Summary for 6UP6

• Entry DOI: 10.2210/pdb6up6/pdb
• EMDB information: 20835
• Descriptor: Endophilin-B1 (1 entity in total)
• Functional Keywords: membrane binding, amphipathic helix, bar protein, sh3 domain, membrane trafficking, cell death, cytosolic protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 44
• Total formula weight: 1797102.82

Authors

Bhatt, V.S.,Sundborger-Lunna, A.C. (deposition date: 2019-10-16, release date: 2020-06-24, Last modification date: 2024-03-20)

Primary citation

Bhatt, V.S.,Ashley, R.,Sundborger-Lunna, A.
Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling.
Structure, 29:61-, 2021

PubMed Abstract: Membrane remodeling is a common theme in a variety of cellular processes. Here, we investigated membrane remodeling N-BAR protein endophilin B1, a critical player in diverse intracellular trafficking events, including mitochondrial and Golgi fission, and apoptosis. We find that endophilin B1 assembles into helical scaffolds on membranes, and that both membrane binding and assembly are driven by interactions between N-terminal helix H0 and the lipid bilayer. Furthermore, we find that endophilin B1 membrane remodeling is auto-inhibited and identify direct SH3 domain-H0 interactions as the underlying mechanism. Our results indicate that lipid composition plays a role in dictating endophilin B1 activity. Taken together, this study provides insight into a poorly understood N-BAR protein family member and highlights molecular mechanisms that may be general for the regulation of membrane remodeling. Our work suggests that interplay between membrane lipids and membrane interacting proteins facilitates spatial and temporal coordination of membrane remodeling.

PubMed: 33086035
DOI: 10.1016/j.str.2020.09.012

Experimental method

ELECTRON MICROSCOPY (9 Å)