Search results for G3BP1

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Species

Types

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Protein (1 results from a total of 1)

Identifier: R-HSA-9729517
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: G3BP1: Q13283

Set (1 results from a total of 1)

Identifier: R-HSA-9729488
Species: Homo sapiens
Compartment: cytosol

Complex (1 results from a total of 1)

Identifier: R-HSA-9729513
Species: Homo sapiens
Compartment: cytosol

Reaction (2 results from a total of 2)

Identifier: R-HSA-9729481
Species: Homo sapiens
Compartment: cytosol
Stress granules (SGs) are dynamic large cytoplasmic mRNA-protein aggregates, formed in response to various stresses, including heat shock, oxidative stress, or viral infection. They can counter viral infection by insulating invaders and limiting viral mRNA translation. SARS-CoV-2 nucleocapsid (N) protein interacts with the SG core component G3BP1/2 (Nabeel-Shah et al. 2020; Gordon et al. 2020; Luo et al. 2021; Wang et al. 2021) and almost completely disrupts SG formation. GST pull-down assays with wild-type and truncated proteins indicated that a fragment from the N-terminal intrinsically disordered region (N-IDR, aa1–48) of N protein and the nuclear transport factor 2 (NTF2) domain of G3BP1are required for the interaction (Huang W et al. 2021). N protein impaired the interaction between G3BP1 and other SG-related proteins and led to SG reconstitution through phase separating with G3BP to occupy protein–protein interaction positions of G3BP (Huang W et al. 2021). It is proposed that N protein-mediated SG disassembly is crucial for SARS-CoV-2 production (Luo et al. 2021; Wang et al. 2021).
Identifier: R-HSA-9694455
Species: Homo sapiens
Compartment: cytosol, endoplasmic reticulum-Golgi intermediate compartment membrane
SARS-CoV-2 nucleocapsid protein (N) can undergo liquid-liquid phase separation (LLPS) with RNA. The mutual interactions between N dimers, and those between N dimers and viral RNA drive a polymerization process leading to compaction of long genomic RNA molecules which is key for viral packaging (Wang S et al. 2021; Cubuk J et al. 2021; Jack et al, 2021; Zhao et al, 2021). The LLPS is robust and binds the SARS-CoV-2 membrane protein (M) (Lu S et al, 2021). It also interacts with the stress granule protein G3BP1, and the TAK1 and IKK complexes, the key kinases of NF-κB signaling, to enhance NF-κB activation (Lu S et al, 2021; Wu Y et al, 2021).
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