Proteopedia

Ras GTPase-activating protein-binding protein


Function

Ras GTPase-activating protein-binding protein (G3BP) is a stress-granule protein that nucletes stress-granule assembly. Stress-granules are sites of mRNA storage that form by stress conditions like viral infection [1].

Disease

G3BP1 can inhibit viral replication and can promote proliferation, invasion and methasthasis of cancer cells[2].

Relevance

Besides G3BP1 implication in cancer, it was found to be functional in neuronal development and maintainance. Hence G3BP1 may function in the progression of neurodegenerative diseases[3].

Structural highlights

G3BP1 contains an N-terminal nuclear transfer factor 2 (NTF2-like) domain, RNA recognition motif domain and Arg-Gly-rich region[4]. The 3D structure of the complex between G3BP1 and Semliki forest virus peptide shows protein:peptide ratio of 2:1. The viral peptide sequence contains twice the tetra peptide FGDF. Each FGDF sequence interacts with one molecule of G3PB1[5]. .

G3BP 3D structures

3D structures of G3BP



Human G3BP1 NTF2-like domain (cyan, green) complex with Semiliki forest virus peptide (pink), sulfate, acetate, glycerol and K+ (PDB 5fw5)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Pandey K, Zhong S, Diel DG, Hou Y, Wang Q, Nelson E, Wang X. GTPase-activating protein-binding protein 1 (G3BP1) plays an antiviral role against porcine epidemic diarrhea virus. Vet Microbiol. 2019 Sep;236:108392. PMID:31500725 doi:10.1016/j.vetmic.2019.108392
  2. ↑ Ge Y, Jin J, Li J, Ye M, Jin X. The roles of G3BP1 in human diseases (review). Gene. 2022 May 5;821:146294. PMID:35176431 doi:10.1016/j.gene.2022.146294
  3. ↑ Sidibé H, Dubinski A, Vande Velde C. The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease. J Neurochem. 2021 May;157(4):944-962. PMID:33349931 doi:10.1111/jnc.15280
  4. ↑ Sidibé H, Dubinski A, Vande Velde C. The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease. J Neurochem. 2021 May;157(4):944-962. PMID:33349931 doi:10.1111/jnc.15280
  5. ↑ Schulte T, Liu L, Panas MD, Thaa B, Dickson N, Gotte B, Achour A, McInerney GM. Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication. Open Biol. 2016 Jul;6(7). pii: 160078. doi: 10.1098/rsob.160078. PMID:27383630 doi:http://dx.doi.org/10.1098/rsob.160078

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