*nlm.life
			PubMed Journals: Biochem Cell Biol

  Source:		PMID: 30943371


    		Biochem Cell Biol. 2019 Apr 3. doi:
     		10.1139/bcb-2018-0394. [Epub ahead of print]

			SARS coronavirus protein nsp1 disrupts localization
			of Nup93 from the nuclear pore complex.

			Gomez GN(1), Abrar F(2), Dodhia MP(3), Gonzalez
			FG(4), Nag A(5).

			Author Information
			(1) Furman University, 3628, Chemistry,
			Greenville, South Carolina, United States
			; garret.gomez@furman.edu.
			(2) Furman University, 3628, Biology, Greenville,
			South Carolina, United States ;
			fabrar95@hotmail.com.
			(3) Furman University, 3628, Greenville,
			South Carolina, United States ;
			maya.dodhia@furman.edu.
			(4) Furman University, 3628, Chemistry,
			Greenville, South Carolina, United States
			; fabby.gonzalez@furman.edu.
			(5) Furman University, 3628, Chemistry and
			Biology, 3300 Poinsett Highway, Greenville,
			South Carolina, United States, 29613-0002
			; anita.nag@furman.edu.

			Severe acute respiratory syndrome coronavirus
			nonstructural protein 1 (nsp1) is a key
			factor in virus-induced down-regulation
			of host gene expression. In infected cells,
			nsp1 engages in a multi-pronged mechanism
			to inhibit host gene expression by binding
			to the 40S ribosome to block the assembly
			of translationally competent ribosome, and
			then inducing endonucleolytic cleavage and
			the degradation of host mRNAs. Here, we
			report a previously undetected mechanism by
			which nsp1 exploits the nuclear pore complex
			and disrupts nuclear-cytoplasmic transport
			of biomolecules. We identified members of
			the nuclear pore complex from nsp1-associated
			protein assembly and found that expression
			of nsp1 in HEK cells disrupts Nup93 localization
			around the nuclear envelope without triggering
			proteolytic degradation, while the nuclear
			lamina remains unperturbed. Consistent with
			its role in host shutoff, nsp1 alters the
			nuclear-cytoplasmic distribution of a RNA
			binding protein, nucleolin. Our results suggest
			that nsp1, alone, can regulate multiple
			steps of gene expression including
			nuclear-cytoplasmic transport.

			DOI: 10.1139/bcb-2018-0394 PMID: 30943371

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