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Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, ar... Show undefined attributes

dbId	179384
displayName	Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, ar...
literatureReference	[LiteratureReference:195606] Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade [LiteratureReference:195621] Nuclear export of influenza virus ribonucleoproteins: identification of an export intermediate at the nuclear periphery [LiteratureReference:195611] Inhibition of nuclear export of ribonucleoprotein complexes of influenza virus by leptomycin B [LiteratureReference:195610] A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction [LiteratureReference:192782] Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes [LiteratureReference:167644] The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP [LiteratureReference:195619] A role for the basic patch and the C terminus of RanGTP in regulating the dynamic interactions with importin beta, CRM1 and RanBP1 [LiteratureReference:195608] Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor [LiteratureReference:166936] Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex [LiteratureReference:195605] Membrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling
modified	[InstanceEdit:197159] Gillespie, ME, 2007-04-30 20:06:36
schemaClass	Summation
text	Viral RNP, bound by M1 and NEP/NS2 interacting with CRM1, are shuttled through the nuclear pore into the cytoplasm (Martin, 1991; O'Neill, 1998; Buolo, 2006). This mechanism may resemble export of HIV-1 ribonucleoprotein, where the HIV-1 Rev export protein interacts with CRM1 (Askjaer, 1998). A number of cofactors are implicated in CRM1-mediated export, including the small GTPase Ran, Ran-binding proteins 1 and 3, and a guanine nucleotide exchange factor (Nilsson, 2001; Nemergut, 2002; Petosa, 2004). Ternary CRM1-cofactor-cargo complexes likely interact transiently with nuclear pore proteins (nucleoporins) as they traverse the pore (reviewed in Suntharalingam, 2003). RanGTP is hydrolyzed to RanGDP in the cytoplasm, an activity that can be stimulated by NEP/NS2 (Akarsu, 2003). Influenza infection activates Raf/MEK/ERK signaling, which is necessary for NEP/NS2-mediated export of viral RNP (Pleschka, 2001; Marjuki, 2006). Influenza vRNP complexes released into the cytoplasm do not re-enter the nucleus, as they are thought to remain bound by M1, preventing re-import (Martin, 1991). It has been suggested that M1 binding of zinc cations could distinguish M1 bound to the vRNP from polymerized, matrix M1 present in nascent virions (Elster, 1994).

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[Reaction:R-HSA-168880] vRNP Export through the nuclear pore

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