6IKO

Crystal structure of mouse GAS7cb

Summary for 6IKO

• Entry DOI: 10.2210/pdb6iko/pdb
• Descriptor: Growth arrest-specific protein 7 (1 entity in total)
• Functional Keywords: phagocytosis, f-bar domain, lipid binding protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 113644.17

Authors

Hanawa-Suetsugu, K.,Itoh, Y.,Kohda, D.,Shimada, A.,Suetsugu, S. (deposition date: 2018-10-16, release date: 2019-10-16, Last modification date: 2023-11-22)

Primary citation

Hanawa-Suetsugu, K.,Itoh, Y.,Ab Fatah, M.,Nishimura, T.,Takemura, K.,Takeshita, K.,Kubota, S.,Miyazaki, N.,Wan Mohamad Noor, W.N.I.,Inaba, T.,Nguyen, N.T.H.,Hamada-Nakahara, S.,Oono-Yakura, K.,Tachikawa, M.,Iwasaki, K.,Kohda, D.,Yamamoto, M.,Kitao, A.,Shimada, A.,Suetsugu, S.
Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7.
Nat Commun, 10:4763-4763, 2019

PubMed Abstract: Phagocytosis is a cellular process for internalization of micron-sized large particles including pathogens. The Bin-Amphiphysin-Rvs167 (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, impose specific morphologies on lipid membranes. Most BAR domain proteins are thought to form membrane invaginations or protrusions by assembling into helical submicron-diameter filaments, such as on clathrin-coated pits, caveolae, and filopodia. However, the mechanism by which BAR domain proteins assemble into micron-scale phagocytic cups was unclear. Here, we show that the two-dimensional sheet-like assembly of Growth Arrest-Specific 7 (GAS7) plays a critical role in phagocytic cup formation in macrophages. GAS7 has the F-BAR domain that possesses unique hydrophilic loops for two-dimensional sheet formation on flat membranes. Super-resolution microscopy reveals the similar assemblies of GAS7 on phagocytic cups and liposomes. The mutations of the loops abolishes both the membrane localization of GAS7 and phagocytosis. Thus, the sheet-like assembly of GAS7 plays a significant role in phagocytosis.

PubMed: 31628328
DOI: 10.1038/s41467-019-12738-w

Experimental method

X-RAY DIFFRACTION (3.756 Å)